Abstract
Throughout the foregoing discussion, it became increasingly evident that the DNA molecule is completely dependent upon proteins for its every action. Replication was seen to proceed only in the presence of a series of enzymes, as did the synthesis of the nucleotides and their modification after incorporation. Even the structuring of the molecule into chromosomes or nucleoids required action from certain proteins. Hence DNA by itself is obviously inert, an attribute that cannot fail to preclude its being the first molecule of life—proteins certainly, and RNAs possibly, had to precede it in living systems. Although its absence of chemical activity bars DNA from further consideration in the search for the properties of the earliest protobiont, its presence should be expected in the genetic apparatus of the most advanced forms. Were the DNA molecule to participate actively in metabolism, it would of necessity undergo molecular changes. But through its inertness it remains stable, and through its stability it is capable of providing the same precise information to generation after generation of cells.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abraham, D. J. 1971. Proposed detailed structural model for tRNA and its geometric relationship to a messenger. J. Theor. Biol. 30: 83–91.
Adams, J. M., and Cory, S. 1970. Untranslated nucleotide sequence at the 5’-end of R17 bacteriophage RNA. Nature. 227: 570–574.
Adams, J. M., and Cory, S. 1975. Modified nucleosides and bizarre 5’-termini in mouse myeloma mRNA. Nature. 255: 28–33.
Adesnik, M., and Darnell, J. E. 1972. Biogenesis and characterization of histone mRNA in HeLa cells. J. Mol. Biol. 67: 397–406.
Ajtkhozhin, M. A., and Akhanov, A. U. 1974. Release of mRNP-particles of the informosome type from polyribosomes of higher plant embryos. FEBS Lett. 41: 275–279.
Allende, J. E., Monro, R., and Lipmann, F. 1964. Resolution of the E. coli. amino acyl sRNA transfer factor into two complementary fractions. Proc. Nat. Acad. Sci. USA. 51: 1211–1216.
Ames, B. N., and Hartman, P. E. 1963. The histidine operon. Cold Spring Harb. Symp. Quant. Biol. 28: 349–356.
Anderson, J. S., Bretscher, M. S., Clark, B. F. C., and Marcher, K. A. 1967. A GTP requirement for binding initiator tRNA to ribosomes. Nature. 215: 490–492.
Arias, I. M., Doyle, D., and Schimke, R. T. 1969. Studies on the synthesis and degradation of proteins of the endoplasmic reticulum of rat liver. J. Biol. Chem. 244: 3303–3315.
Attardi, G., Huang, P. C., and Kabat, S. 1965. Recognition of rRNA sites in DNA. Proc. Nat. Acad. Sci. USA. 53: 1490–1498.
Averner, M. J., and Pace, N. R. 1972. The nucleotide sequence of marsupial 5 S ribosomal RNA. J. Biol. Chem. 247: 4491–4493.
Ayuso-Parilla, M., Henshaw, E. C., and Hirsch, C. A. 1973a. The ribosome cycle in mammalian protein synthesis. J. Biol. Chem. 248: 4386–4393.
Ayuso-Parilla, M., Hirsch, C. A., and Henshaw, E. C. 1973b. Release of the nonribosomal proteins from the mammalian native 40S ribosomal subunit by aurintricarboxylic acid. J. Biol. Chem. 248: 4394–4399.
Bag, J., and Sarkar, S. 1975. Cytoplasmic nonpolysomal mRNP containing actin mRNA in chicken embryonic muscles. Biochemistry. 14: 3800–3807.
Ball, L. A. 1973. Mutual influence of the secondary structure and informational content of a mRNA. J. Theor. Biol. 4: 243–247.
Barrieux, A., Ingraham, H. A., David, D. N., and Rosenfeld, M. G. 1975. Isolation of messenger-like RNPs. Biochemistry. 14:1815–1821.
Beaudet, A. L., and Caskey, C. T. 1971. Mammalian peptide chain termination. Proc. Nat. Acad. Sci. USA. 68: 619–624.
Bell, E., and Reeder, R. 1965. Short-and long-lived mRNA in embryonic chick lens. Science. 150: 71–72.
Bellmare, G., Jordan, B. R., Rocca-Serra, J., and Monier, R. 1972. Accessibility of E. coli. 5. S RNA base residues to chemical reagents. Biochimie. 54: 1453–1466.
Bellmare, G., Vigne, R., and Jordan, B. R. 1973. Interaction between E. coli. ribosomal proteins and 5 S RNA molecules. Biochimie. 55: 29–35.
Benhamou, J., and Jordan, B. R. 1976. Nucleotide sequence of D. melanogaster. 5. S RNA. FEBS Lett. 62: 146–149.
Benhamou, J., Jourdan, R., and Jordan, B. R. 1977. Sequence of Drosophila. 5. S RNA synthesized by cultured cells and by the insect at different developmental stages. J. Mol. Evol. 9: 279–298.
Berns, A. J. M., Strous, G. J. A. M., and Bloemendal, H. 1972. Heterologous in vitro. synthesis of lens a-crystallin polypeptide. Nature New Biol. 236: 7–9.
Billeter, M. A., Dahlberg, J. E., Goodman, H. E., Hindley, J., and Weissmann, C. 1969. Sequence of first 175 nucleotides from the 5’-terminus of Qß RNA synthesized in vitro. Nature. 224: 1083–1086.
Bishop, J. O., Morton, J. G., Rosbach, M., and Richardson, M. 1974. Three abundance classes in HeLa cell mRNA. Nature. 250: 199–204.
Bitar, K. G. 1975. The primary structure of the ribosomal protein L29 from E. coli. Biochim. Biophys. Acta. 386: 99–106.
Bitar, K. G., and Wittmann-Liebold, B. 1975. The primary structure of the 5 S rRNA binding protein L25 of E. coli. Hoppe-Seyler’s Zeit. Phys. Chem. 356: 1343–1352.
Blobel, G. 1972. Protein tightly bound to globin mRNA. Biochem. Biophys. Res. Comm. 47: 88–95.
Blobel, G. 1973. A protein of molecular weight 78,000 bound to the poly(A) region of eukaryotic mRNAs. Proc. Nat. Acad. Sci. USA. 70: 924–928.
Bloemendal, H. 1977. The vertebrate eye lens. Science. 197: 127–138.
Blundell, M., Craig, E., and Kennell, D. 1972. Decay rates of different mRNA in E. coli. and models of decay. Nature New Biol. 238: 46–49.
Bollini, R., Soffientini, A. N., Bertani, A., and Lanzani, G. A. 1974. Some molecular properties of the elongation factor EF-1 from wheat embryos. Biochemistry. 13: 5421–5425.
Bonnet, J., and Ebel,.1. P. 1972. Interpretation of incomplete reactions in tRNA aminoacylation. Aminoacylation of yeast tRNAva’ with yeast valyl-tRNA synthetase. Eur. J. Biochem. 31: 335–344.
Bonnet, J., and Ebel, J. P. 1974. Correction of aminoacylation errors: evidence for a nonsignificant role of the aminoacyl-tRNA synthetase catalyzed deacylation of aminoacyl-tRNAs. FEBS Lett. 39: 259–262.
Bonnet, J., Giegé, R., and Ebel, J. P. 1972. Lack of specificity in the aminoacyl-tRNA synthetasecatalysed deacylation of aminoacyl-tRNA. FEBS Lett. 27: 139–144.
Bostock, C. J., Prescott, D. M., and Lauth, M. 1971. Lability of 26 S rRNA in Tetrahymena pyriformis. Exp. Cell Res. 66: 260–262.
Branlant, C., and Ebel, J.-P. 1977. Studies on the primary structure of E. coli. 23 S RNA. Nucleotide sequence of the ribonuclease Tl digestion products containing more than one uridine residue. J. Mol. Biol. 111: 215–256.
Brenner, S., Jacob, F., and Meselson, M. 1961. An unstable intermediate carrying information from genes to ribosomes for protein synthesis. Nature. 190: 576–581.
Bretscher, M. S. 1965. Fractionation of oligolysyl-adenosine complexes derived from polylysine attached to tRNA. J. Mol. Biol. 12: 913–919.
Bretscher, M. S. 1966. Polypeptide chain initiation and the characterization of ribosomal binding in E. coli. Cold Spring Harbor Symp. Quant. Biol. 31: 289–296.
Bretscher, M. S. 1968. Direct translation of a circular mRNA. Nature. 220: 1088–1091.
Bretscher, M. S. 1969. Direct translation of bacteriophage fd DNA in the absence of neomycin B. J. Mol. Biol. 42: 595–598.
Bretscher, M. S., Goodman, H. M., Menninger, J. R., and Smith, J. D. 1965. Polypeptide chain termination using synthetic polynucleotides. J. Mol. Biol. 14: 634–639.
Brinacombe, R., Nierhaus, K. H., Garrett, R. A., and Wittmann, H. G. 1976. The ribosome of E. coli. Progr. Nucl. Acid Res. Mol. Biol. 18:1–44, 323–325.
Brosius, J., and Chen, R. 1976. The primary structure of protein L16 located at the peptidyl-transferase center of E. coli. ribosomes. FEBS Lett. 68: 105–109.
Brosius, J., Schiltz, E., and Chen, R. 1975. The primary structure of the 5 S RNA binding protein L18 from E. coli. ribosomes. FEBS Lett. 56: 359–361.
Brot, N., Tate, W. P., Caskey, C.-T., and Weissbach, H. 1974. The requirement for ribosomal proteins L7 and L12 in peptide-chain termination. Proc. Nat. Acad. Sci. USA. 71: 89–92.
Brouwer, J., and Planta, R. J. 1975. The origin of high molecular weight proteins in ribosomal preparations of Bacillus licheniformis. FEBS Lett. 53: 73–75.
Brown, D. D., and Weber, C. S. 1968. Unique DNA sequences homologous to 4 S RNA, 5 S RNA, and rRNA. J. Mol. Biol. 34: 661–680.
Brown, D. D., Wensink, P. C., and Jordan, E. 1971. Purification and some characteristics of 5 S DNA from Xenopus laevis. Proc. Nat. Acad. Sci. USA. 68: 3175–3179.
Brown, G. L. 1963. Preparation, fractionation, and properties of sRNA. Progr. Nucl. Acid Res. 2: 259–310.
Brown, J. C., and Doty, P. 1968. Protein factor requirement for binding of mRNA to ribosomes. Biochem. Biophys. Res. Comm. 30: 284–291.
Brownlee, G. G., Cartwright, E., McShane, T., and Williamson, R. 1972. The nucleotide sequence of somatic 5 S RNA from Xenopus laevis. FEBS Lett. 25: 8–12.
Brownlee, G. G., Sanger, F., and Barrell, B. G. 1967. Nucleotide sequence of 5 S rRNA from E. coli. Nature. 215: 735–736.
Brownlee, G. G., Sanger, F., and Barrell, B. G. 1968. The sequence of 5 S rRNA. J. Mol. Biol. 34: 379–412.
Bryan, R. N., and Hayashi, M. 1973. Two proteins are bound to most species of polysomal mRNA. Nature New Biol. 244: 271–274.
Buckingham, M. E., Caput, D., Cohen, A., Whalen, R. G., and Gros, F. 1974. The synthesis and stability of cytoplasmic mRNA during myoblast differentiation in culture. Proc. Nat. Acad. Sci. USA. 71. :1466–1470.
Burr, H., and Lingrel, J. B. 1971. Poly A sequences at the 3’ termini of rabbit globin mRNAs. Nature New Biol. 233: 41–43.
Burstein, Y., Kantor, F., and Schechter, I. 1976. Partial amino-acid sequence of the precursor of an immuno-globulin light chain containing NH2-terminal pyroglutamic acid. Proc. Nat. Acad. Sci. USA. 73: 2604–2608.
Busby, W. F., Hele, P., and Chang, M. C. 1974. Apparent amino acid incorporation by ejaculated rabbit spermatozoa. Biochim. Biophys. Acta. 330: 246–259.
Busiello, E., and DiGirolamo, M. 1973. Aminoacyl-tRNA binding sites in E. coli. and reticulocyte ribosomes. FEBS Lett. 35: 341–343.
Campo, M. S., and Bishop, J. O. 1974. Two classes of mRNA in cultured rat cells. J. Mol. Biol. 90: 649–663.
Cann, A., Gambino, R., Banks, J., and Bank, A. 1974. Poly(A) sequences and biological activity from human globin mRNA. J. Biol. Chem. 249: 7536–7540.
Cantor, C. R. 1967. Possible conformations of 5 S rRNA. Nature. 216: 513–514.
Cantor, C. R. 1968. The extent of base pairing in 5 S rRNA. Proc. Nat. Acad. Sci. USA. 59: 478–483.
Cashion, L. M., and Stanley, W. M. 1974. Two eukaryotic initiation factors (IF-I and IF-II) of protein synthesis that are required to form an initiation complex with rabbit reticulocyte ribosomes. Proc. Nat. Acad. Sci. USA. 71: 436–440.
Caskey, C. T. 1973. Peptide chain termination. Adv. Prot. Chem. 27: 243–276.
Caskey, C. T., Beaudet, A. L., and Tate, W. P. 1974. Mammalian release factor. Methods Enzymol. 30: 293–303.
Caskey, T., Leder, P., Moldave, K., and Schlessinger, D. 1972. Translation: Its mechanism and control. Science. 176: 195–197.
Ceccarini, C., and Maggio, R. 1968. Studies on the ribosomes from the cellular slime molds, Dictyostelium discoideum. and D. purpureum. Biochim. Biophys. Acta. 166: 134–141.
Cedergren, R. J., and Sankoff, D. 1976. Evolutionary origin of 5.8 S rRNA. Nature. 260:74–75. Chambers, R. W. 1971. On the recognition of tRNA by its aminoacyl-tRNA ligase. Progr. Nucl. Acid Res. 11: 489–525.
Chatterjee, S. K., Kazemie, M., and Matthaei, H. 1973. Separation of the ribosomal proteins by two-dimensional electrophoresis. Hoppe-Seyler’s Z. Phys. Chem. 354: 481–486.
Chen, R., and Ehrke, G. 1976. The primary structure of protein L34 from the large ribosomal subunit of E. coli. FEBS Lett. 63: 215–217.
Chen, R., Mende, L., and Arfsten, U. 1975. The primary structure of protein L27 from the peptidyl-tRNA binding site of E. coli. ribosomes. FEBS Lett. 59: 96–99.
Chen, R., and Wittmann-Liebold, B. 1975. The primary structure of protein S9 from the 30 S subunit of E. coli. ribosomes. FEBS Lett. 52: 139–140.
Cimadevilla, J. M., and Hardesty, B. 1975. Isolation and partial characterization of a 40 S riboso- mal subunit-tRNA binding factor from rabbit reticulocytes. J. Biol. Chem. 250: 4389–4397.
Clark, B. F. C., and Marcker, K. A. 1966. The role of N-formyl-methionyl-sRNA in protein biosynthesis. J. Mol. Biol. 17: 394–406.
Cole, P. E., and Crothers, D. H. 1972. Conformational changes of tRNA. Biochemistry. 11: 4368–4374.
Cole, P. E., Young, S. K., and Crothers, D. M. 1972. Conformational changes of tRNA. Equilibrium phase diagrams. Biochemistry. 11: 4358–4368.
Comb, D. G., and Sarkar, N. 1967. The binding of 5 S rRNA to ribosomal subunits. J. Mol. Biol. 25: 317–330.
Contreras, R., Vandenberghe, A., Min Jou, W., de Wachter, R., and Fiers, W. 1971. Studies on the bacteriophage MS2 nucleotide sequence of a 3’-terminal fragment (n =. 104). FEBS Lett. 18: 141–144.
Contreras, R., Ysebaert, M., Min Jou, W., and Fiers, W. 1973. Bacteriophage MS2 RNA: nucleotide sequence of the end of the A protein gene on the intercistronic region. Nature New Biol. 241: 99–101.
Conway, T. W., and Lipmann, F. 1964. Characterization of a ribosome-linked guanosine triphosphatase in E. coli. extracts. Proc. Nat. Acad. Sci. USA. 52: 1462–1469.
Cornick, G. G., and Kretsinger, R. H. 1977. The 30 S subunit of the E. coli. ribosome. Biochim. Biophys. Acta. 474: 398–410.
Corry, M. J., Payne, P. I., and Dyer, T. A. 1974a. The nucleotide sequence of 5 S rRNA from the blue-green alga Anacystis nidulans. FEBS Lett. 46: 63–66.
Cony, M. J., Payne, P. I., and Dyer, T. A. 1974b. A sequence analysis of 5 S rRNA from the blue-green alga Oscillatoria tenuis. and a comparison of blue-green alga 5 S rRNA with those of bacterial and eukaryotic origin. FEBS Lett. 46: 67–70.
Cox, R. A. 1970. A spectrophotometric study of the secondary structure of RNA isolated from the smaller and larger ribosomal subparticles of rabbit reticulocytes. Biochem. J. 117: 101–118.
Cox, R. A., Gould, H., and Kanagalingam, K. 1968. A study of the alkaline hydrolysis of fractionated reticulocyte rRNA and its relevance to secondary structure. Biochem. J. 106: 733–741.
Cramer, F. 1969. Three-dimensional structure of tRNA. Progr. Nucl. Acid. Res. 11: 391–421.
Cramer, F., and Erdman, V. A. 1968. Amount of adenine and uracil base pairs in E. coli. 23 S, 16 S, and 5 S rRNA. Nature. 218: 92–93.
Cremer, K., and Schlessinger, D. 1974. Ca’ ions inhibit mRNA degradation but permit mRNA transcription and translation in DNA-coupled systems from E. coli. J. Biol. Chem. 249: 4730–4736.
Crick, F. H. C. 1966. The genetic code: Yesterday, today, and tomorrow. Cold Spring Harbor Symp. Quant. Biol. 31: 3–10.
Crick, F. H. C. 1967. The genetic code. Proc. Roy. Soc. London. B167: 331–347.
Crick, F. H. C., Barnett, L., Brenner, S., and Watts-Tobin, R. J. 1961. General nature of the genetic code for proteins. Nature. 192: 1227–1232.
Crystal, R. A., and Anderson, W. F. 1972. Initiation of hemoglobin synthesis. Proc. Nat. Acad. Sci. USA. 69: 706–711.
Crystal, R. A., Elson, N. A., and Anderson, W. F. 1974. Initiation of globin synthesis. Methods Enzymol. 30: 101–127.
Czernilofsky, A. P., Collatz, E. E., Stöffler, G., and Kuechler, E. 1974. Proteins at the tRNA binding sties of E. coli. ribosomes. Proc. Nat. Acad. Sci. USA. 71: 230–234.
Dahlberg, A. E. 1974. Two forms of the 30 S ribosomal subunit of E. coli. J. Biol. Chem. 249: 7673–7678.
Darnell, J. E., Wall, R., and Tushinski, R. J. 1971. An adenylic acid-rich sequence in mRNA of HeLa cells and its possible relationship to reiterated sites in DNA. Proc. Nat. Acad. Sci. USA. 68: 1321–1325.
Davidson, J. N. 1972. The Biochemistry of the Nucleic Acids. 7th Ed., New York, Academic Press.
Daya-Grosjean, L., Reinbolt, J., Pongs, O., and Garrett, R. A. 1974. A study of the regions of ribosomal proteins S4, S8, S15, and S20 that interact with 16 S RNA of E. coli. FEBS Lett. 44: 253–256.
Dayhoff, M. O. 1972. Atlas of Protein Sequence and Structure. 1972. Washington, National Biomedical Research Foundation.
Diez, J., and Brawerman, G. 1974. Elongation of the poly(A) segment of mRNA in the cytoplasm of mammalian cells. Proc. Nat. Acad. Sci. USA. 71: 4091–4095.
Dillon, L. S. 1962. Comparative cytology and the evolution of life. Evolution. 16: 102–117.
Dillon, L. S. 1963. A reclassification of the major groups of organisms based upon comparative cytology. Syst. Zool. 12: 71–82.
Dillon, L. S. 1973. The origins of the genetic code. Bot. Rev. 39: 301–345.
Dillon, L. S. 1978. Evolution: Concepts and Consequences. 2nd Ed., St. Louis, Mo., C. V. Mosby Co.
Dina, D., Crippa, M., and Beccari, E. 1973. Hybridization properties and sequence arrangement in a population of mRNAs. Nature New Biol. 242: 101–105.
Dina, D., Meza, I., and Crippa, M. 1974. Relative positions of the `repetitive,’ `unique’ and poly(A) fragments of mRNA. Nature. 248: 486–490.
Dohme, F., and Nierhaus, K. H. 1976. Role of 5 S RNA in assembly and function of the 50 S subunit from E. coli. Proc. Nat. Acad. Sci. USA. 73: 2221–2225.
Dovgas, N. V., Markova, L. F., Mednikova, T. A., Vinokurov, L. M., Alakhov, Y. B., and Ovchinnihov, Y. A. 1975. The primary structure of the 5 S RNA binding protein L25 from E. coli. ribosomes. FEBS Lett. 53: 351–354.
Dovgas, N. V., Vinokurov, L. M., Velmoga, I. S., Alakhov, Y. B., and Ovchinnikov, Y. A. 1976. The primary structure of protein L10 from E. coli. ribosomes. FEBS Lett. 67: 58–61.
Drews, J., Bednarik, K., and Grasmuck, H. 1974. Elongation factor 1 from Krebs H mouse ascites cells. Eur. J. Biochem. 41: 217–227.
Dube, S. K. 1973. Recognition of tRNA by the ribosome. A possible role of 5 S RNA. FEBS Lett. 36: 39–42.
Dubuy, B., and Weissman, S. M. 1971. Nucleotide sequence of Pseudomonas fluorescens. 5. S RNA. J. Biol. Chem. 246: 747–761.
Dworkin, M. B., Rudensey, L. M., and Infante, A. A. 1977. Cytoplasmic nonpolysomal RNP particles in sea urchin embryos and their relationship to protein synthesis. Proc. Nat. Acad. Sci. USA. 74: 2231–2235.
Ebel, J. P., Geigé, R., Bonnet, J., Kern, D., Befort, N., Bollack, C., Fasiolo, F., Gangloff, J., and Dirheimer, G. 1973. Factors determining the specificity of the tRNA aminoacylation reaction. Biochimie. 55: 547–557.
Edmunds, M., Vaughan, M. H., and Nakazato, H. 1971. Poly(A) sequences in the hnRNA and rapidly-labelled polyribosomal RNA of HeLa cells. Proc. Nat. Acad. Sci. USA. 68: 1336–1340.
Edström, J.-E., and Tanguay, R. 1974. Cytoplasmic RNAs with messenger characteristics in salivary gland cells of Chironomus tentans. J. Mol. Biol. 84: 569–583.
Ehrenfeld, E., and Summers, D. 1972. Adenylate-rich sequences in vesicular stomatitis virus mRNA. J. Virol. 10: 683–688.
Ehresmann, C., Fellner, P., and Ebel, J. P. 1970. Nucleotide sequences of sections of 16 S rRNA. Nature. 227: 1321–1323.
Ehresmann, C., Steigler, P., Fellner, P., and Ebel, J. P. 1975. The determination of the primary structure of the 16 S ribosomal RNA of E. coli. III. Further studies. Biochimie. 57: 71 1748.
Eisenstadt, J. M., and Brawerman, G. 1967. The role of the native subribosomal particles of E. coli. in polypeptide chain initiation. Proc. Nat. Acad. Sci. USA. 58: 1560–1565.
Erdmann, V. A. 1976. Structure and function of 5 S and 5.8 S RNA. Progr. Nucl. Acid Res. Mol. Biol. 18: 45–90.
Erdmann, V. A., Sprinzl, M., and Pongs, O. 1973. The involvement of 5 S RNA in the binding of tRNAs to ribosomes. Biochem. Biophys. Res. Comm. 54: 942–948.
Eremenko, T., and Volpe, P. 1975. Polysome translational state during the cell cycle. Eur. J. Biochem. 52: 203–210.
Fakunding, J. L., Traut, R. R., and Hershey, J. W. B. 1973. Dependence of initiation factor IF-2 activity on proteins L7 and L12 from E. coli. 50 S ribosomes. J. Biol. Chem. 248: 8555–8559.
Fakunding, J. L., Trough, J. A., Traut, R. R., and Hershey, J. W. B. 1974. Purification and phosphorylation of initiation factor IF2. Meth. Enzym. 30: 24–31.
Favre, A., Morel, C., and Scherrer, K. 1975. The secondary structure and poly(A) content of globin mRNA as a pure RNA and in polyribosome-derived RNP complexes. Eur. J. Biochem. 57: 147–157.
Fellner, P., and Ebel, J. P. 1970. Observations on the primary structure of the 23 S rRNA from E. coli. Nature. 225: 1131–1132.
Fellner, P., Ehresmann, C., and Ebel, J. P. 1970. Nucleotide sequences present within the 16 S rRNA of E. coli. Nature. 225: 26–29.
Fellner, P., Ehresmann, C., and Ebel, J. P. 1972a. The determination of the primary structure of the 16 S rRNA of E. coli. I. Nucleotide sequence analysis of T1 and pancreatic RNase digestion products. Biochimie. 54: 853–900.
Fellner, P., Ehresmann, C., Stiegler, P., and Ebel, J. P. 1972b. Partial nucleotide sequence of 16 S rRNA from E. coli. Nature New Biol. 239: 1–5.
Fellner, P., and Sanger, F. 1968. Sequence analysis of specific areas of the 16 S and 23 S rRNAs. Nature. 219: 236–238.
Fiers, W., Contreras, R., de Wachter, R., Haegeman, G., Merregaert, J., Min Jou, W., and Vandanberghe, A. 1971. Recent progress in the sequence determination of bacteriophage MS2 RNA. Biochimie. 53: 495–506.
Fiers, W., Contreras, R., Duerinck, F., Haegeman, G., Iserentant, D., Merregaert, J., Min Jou, W., Molemans, F., Racymackers, A., Van der Bergh, A., Volckaert, G., and Ysebaert, M. 1976. Complete nucleotide sequence of bacteriophage MS2 RNA: Primary and secondary structure of the replicase gene. Nature. 260: 500–507.
Firtel, R. A., Jacobson, A., and Lodish, H. F. 1972. Isolation and hybridization kinetics of mRNA from Dictyostelium discoideum. Nature New Biol. 239: 225–228.
Fischel, J. L., and Ebel, J. P. 1975. Sequence studies on the 5 S RNA of Proteus vulgaris: Comparison with the 5 S of E. coli. Biochimie. 57: 899–904.
Fiser, I., Scheit, K. H., Stöffler, G., and Kuechler, E. 1974. Identification of protein S1 at the mRNA binding site of the E. coli. ribosome. Biochem. Biophys. Res. Comm. 60: 1112–1118.
Florendo, N. T. 1969. Ribosome substructure in intact mouse liver cells. J. Cell Biol. 41: 335–339.
Ford, P. J., and Southern, E. M. 1973. Different sequences for 5 S RNA in kidney cells and ovaries of Xenopus laevis. Nature New Biol. 241: 7–12.
Forget, B. G., and Jordan, B. 1969.5 S RNA synthesized by E. coli. in presence of chloramphenicol. Science. 167: 382–384.
Forget, B. G., and Weissman, S. M. 1967. Nucleotide sequence of KB cell 5 S RNA. Science. 158: 1695–1699.
Forget, B. G., and Weissman, S. M. 1969. The nucleotide sequence of ribosomal 5 S RNA from KB cells. J. Biol. Chem. 244: 3148–3165.
Forget, B. G., Housman, D., Benz, E. J., and McCaffrey, R. P. 1975. Synthesis of DNA complementary to separated human a and ß globin mRNAs. Proc. Nat. Acad. Sci. USA. 72: 984–988.
Fouquet, H., and Sauer, H. W. 1975. Variable redundancy in RNA transcripts isolated in S and G2 phase of the cell cycle of Physarum. Nature. 255: 253–255.
Fox, G. E., and Woese, C. R. 1975. 5 S RNA secondary structure. Nature. 256: 505–507.
Fromson, D., and Duchastel, A. 1975. Poly(A)-containing polyribosomal RNA in sea urchin embryos. Biochim. Biophys. Acta. 378: 394–404.
Fromson, D., and Verma, D. P. S. 1976. Translation of nonpolyadenylated mRNA of sea urchin embryos. Proc. Nat. Acad. Sci. USA. 73. :148–151.
Fujisawa, T., and Eliceiri, G. L. 1975. Ribosomal proteins of hamster, mouse, and hybrid cells. Biochim. Biophys. Acta. 402: 238–243.
Funatsu, G., Yaguchi, M., and Wittmann-Liebold, B. 1977. Primary structure of protein S 12 from the small E. coli. ribosomal subunit. FEBS Lett. 73: 12–17.
Ganoza, M. C., and Fox, J. L. 1974. Isolation of a soluble factor needed for protein synthesis with various messenger ribonucleic acids other than poly(U). J. Biol. Chem. 249: 1037–1043.
Garen, A. 1968. Sense and nonsense in the genetic code. Science. 160: 149–159.
Garrett, R. A., Schulte, C., Stöffler, G., Gray, P., and Monier, R. 1974. The release of proteins and 5 S RNA during the unfolding of E. coli. ribosomes. FEBS Lett. 49: 1–4.
Garrett, R. A., and Wittmann, H. G. 1973. Structure of bacterial ribosomes. Adv. Prot. Chem. 27: 277–347.
Gasior, E., and Moldave, K. 1972. Evidence for a soluble protein factor specific for the interaction between aminoacylated tRNAs and the 40 S subunit of mammalian ribosomes. J. Mol. Biol. 66: 391–402.
Georgiev, G. P., and Samarina, O. P. 1971. D-RNA containing RNP particles. Adv. Cell Biol. 2: 47–110.
Gesteland, R. F. 1966. Unfolding of E. coli. ribosomes by removal of magnesium. J. Mol. Biol. 18: 356–371.
Ghosh, H. P., and Khorana, H. G. 1967. On the role of ribosomal subunits in protein synthesis. Proc. Nat. Acad. Sci. USA. 58: 2455–2461.
Ghosh, H. P., Söll, D., and Khorana, H. G. 1967. Initiation of protein synthesis in vitro. as studied by using ribopolynucleotide with repeating nucleotide sequences as messengers. J. Mol. Biol. 25: 275–298.
Gillespie, D., Takemoto, K., Robert, M., and Gallo, R. C. 1973. Poly(A) in visna virus RNA. Science. 179: 1328–1330.
Ginzburg, I., and Zanier, A. 1975. Characterization of different conformational forms of 30 S ribosomal subunits in isolated and associated states. J. Mol. Biol. 93: 465–476.
Glazier, K., and Schlessinger, D. 1974. Magic spot metabolism in an E. coli. mutant temperature sensitive in elongation factor Ts. J. Bact. 117: 1195–1200.
Glick, B. R. 1977. The role of E. coli. ribosomal proteins L7 and L12 in peptide chain elongation. FEBS Lett. 73. :1–5.
Glick, B. R., and Ganoza, M. C. 1976. Characterization and site of action of a soluble protein that stimulates peptide-bond synthesis. Eur. J. Biochem. 71: 483–491.
Goldberg, A. L., and Wittes, R. E. 1966. Genetic code: Aspects of organization. Science. 153: 420–424.
Goodman, H. M., Billeter, M. A., Hindley, J., and Weissmann, C. 1970. The nucleotide sequence at the 5’-terminus of the Qß RNA minus strand. Proc. Nat. Acad. Sci. USA. 67: 921–928.
Gordon, J., Schweiger, M., Krisko, I., and Williams, C. A. 1969. Specificity and evolutionary divergence of the antigenic structure of the polypeptide chain elongation factors. J. Bact. 100: 1–4.
Gormly, J. R., Yang, C. H., and Horowitz, J. 1971. Further studies on ribosome unfolding. Biochim. Biophys. Acta. 247: 80–90.
Gorski, J., Morrison, M. R., Merkel, C. G., and Lingrel, J. B. 1975. Poly(A) size class distribution in globin mRNAs as a function of time. Nature. 253: 749–751.
Gottlieb, M., Lubsen, N. H., and Davis, B. D. 1974. Ribosome dissociation factors. Methods Enzymol. 30: 87–94.
Gould, R. M., Thornton, M. P., Liepkalns, V., and Lennarz, W. J. 1968. Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidyiglycerol synthesis. J. Biol. Chem. 243: 3096–3104.
Gralla, J., and De Lisi, C. 1974. mRNA is expected to form stable secondary structures. Nature. 248: 330–332.
Gralla, J., Steitz, J. A., and Crothers, D. M. 1974. Direct physical evidence for secondary structure in an isolated fragment of R17 bacteriophage mRNA. Nature. 248: 204–208.
Grasmuck, H., Nolan, R. D., and Drews, J. 1974. Elongation factor 1 from ascites tumor cells. Eur. J. Biochem. 48: 485–493.
Grasmuk, H., Nolan, R. D., and Drews, J. 1976. A new concept of the function of EF-1 in peptide chain elongation. Eur. J. Biochem. 71: 271–279.
Gray, M. W. 1974. The presence of 02 -methylpseudouridine in the 18 S + 26 S ribosomal ribonucleates of wheat embryo. Biochemistry. 13: 5453–5463.
Grayson, S., and Berry, S. J. 1973. Estimation of the half-life of a secretory protein message. Science. 180: 1071–1072.
Greenberg, J. R. 1975. Messenger RNA metabolism of animal cells. J. Cell Biol. 64: 269–288.
Greenberg, J. R. 1976. Isolation of L-cell mRNA which lacks poly(A). Biochemistry. 15: 3516–3552.
Greenberg, J. R., and Perry, R. P. 1972. Relative occurrence of poly(A) sequences in messenger and hnRNA of L cells as determined by poly(U)-hydroxylapatite chromatography. J. Mol. Biol. 72: 91–98.
Grierson, D. 1974. Characterization of RNA components from leaves of Phaseolus aureus. Eur. J. Biochem. 44: 509–515.
Gross, P. R., and Cousineau, G. H. 1963. Effects of actinomyin D on macromolecule synthesis and early development in sea urchin eggs. Biochem. Biophys. Res. Comm. 10: 321–326.
Groves, W. E., and Kempner, E. S. 1967. Amino acid coding in Sarcina lutea. and Saccharomyces cerevisiae. Science. 156: 387–390.
Grozdanovic, J., and Hradec, J. 1975. Different binding sites of poly(A)-containing and poly(A)free fractions of nuclear ribonucleic acid to ribosomes from rat liver. Biochem. Biophys. Acta. 402: 69–82.
Gualerzi, C., Janda, H. G., Passow, H., and Stöffler, G. 1974. Studies on the protein moiety of plant ribosomes. J. Biol. Chem. 249: 3347–3355.
Gualerzi, C., Pon, C. L., and Kaji, A. 1971. Initiation factor dependent release of aminoacyltRNAs from complexes of 30 S ribosomal subunits, synthetic polynucleotide and aminoacyl tRNA. Biochem. Biophys. Res. Comm. 45: 1312–1319.
Gurdon, J. B., Lane, C. D., Woodland, H. R., and Marbaix, G. 1971. Use of frog eggs and oocytes for the study of mRNA and its translation in living cells. Nature. 233: 177–182.
Haenni, A. L., and Lucas-Lenard, J. 1970. Function of the elongation factors T and G. In: Ochoa, S., C. F. Heredin, C. Asensio, and D. Nachmansohn, eds., Macromolecules: Biosynthesis and Function., New York, Academic Press, p. 97–108.
Haguenau, F. 1958. The ergastoplasm: Its history, ultrastructure and biochemistry. Internat. Rev. Cytol. 7: 425–483.
Haines, M. E., Carey, N. H., and Palmiter, R. D. 1974. Purification and properties of ovalbumin mRNA. Eur. J. Biochem. 43: 549–560.
Hall, N. D., and Amstein, H. R. V. 1973. Specificity of reticulocyte initiation factors for the translation of globin mRNA. Biochem. Biophys. Res. Comm. 54: 1489–1497.
Hamel, E., and Cashel, M. 1973. Role of guanine nucleotides in protein synthesis. Proc. Nat. Acad. Sci. USA. 70: 3250–3254.
Hampel, A., and Enger, M. D. 1973. Subcellular distribution of aminoacyl-transfer RNA synthetases in Chinese hamster ovary cell culture. J. Mol. Biol. 79: 285–293.
Hardy, S. J. S., Kurland, C. G., Voynow, P., and Mora, G. 1969. The ribosomal proteins of E. coli. Biochemistry. 8: 2897–2905.
Hasselkorn, R., and Rothman-Denes, L. B. 1973. Protein synthesis. Ann. Rev. Biochem. 42: 397–438.
Hatfield, D. 1972. Recognition of nonsense codons in mammalian cells. Proc. Nat. Acad. Sci. USA. 69: 3014–3018.
Hatlen, L., and Attardi, G. 1971. Proportion of the HeLa cell genome complementary to tRNA and 5 S RNA. J. Mol. Biol. 56: 535–554.
Hattman, S., and Hofschneider, P. H. 1968. Influence of T4 on the formation of RNA phage-specific polyribosomes and polymerase. J. Mol. Biol. 35: 513–522.
Hawley, D. A., Miller, M. J., Slobin, L. I., and Wahba, A. J. 1974. The mechanism of action of initiation factor 3 in protein synthesis. Biochem. Biophys. Res. Comm. 61: 329–337.
Held, W. A., Getle, W. R., and Nomura, M. 1974. Role of 16 S ribosomal RNA and the 30 S ribosomal protein S12 in the initiation of natural mRNA translation. Biochemistry. 13: 2115–2122.
Hellerman, J. G., and Shafritz, D. A. 1975. Initiation of poly(A) and mRNA with eukaryotic initiator Met tRNAf binding factor. Proc. Nat. Acad. Sci. USA. 72: 1021–1025.
Hemminki, K. 1974. Poly(A) in RNA extracted by thermal phenol fractionation from chick embryo brain and liver. Biochim. Biophys. Acta. 340: 262–268.
Henriksen, O., Robinson, E. A., and Maxwell, E. S. 1975a. Interaction of guanosine nucleotides with EF-2. I. Equilibrium dialysis studies. J. Biol. Chem. 250: 720–724.
Henriksen, O., Robinson, E. A., and Maxwell, E. S. 1975b. Interaction of guanosine nucleotides with EF-2. II. Effects of ribosomes and magnesium ions on guanosine diphosphate and guano-sine triphosphate binding to the enzyme. J. Biol. Chem. 250: 725–730.
Henshaw, E. C., Guiney, D. G., and Hirsch, C. A. 1973. The ribosome cycle in mammalian protein synthesis. J. Biol. Chem. 248: 4367–4376.
Herr, W., and Noller, H. F. 1975. A fragment of 23 S RNA containing a nucleotide sequence complementary to a region of 5 S RNA. FEBS Lett. 53: 248–252.
Herrington, M. D., and Hawtrey, A. O. 1971. Differences in the ribosomes prepared from lactating and non-lactating bovine mammary gland. Biochem. J. 121: 279–285.
Hershey, A. D., Dixon, J., and Chase, M. 1953. Nucleic acid economy in bacteria infected with bacteriophage T2. J. Gen. Physiol. 36: 777–789.
Hershey, J. W. B., Dewey, K. F., and Thach, R. E. 1969. Purification and properties of IF-1. Nature. 222: 944–947.
Highland, J. H., Bodley, J. W., Gordon, J., Hasenbank, R., and Stöffler, G. 1973. Identity of the ribosomal proteins involved in the interaction with EF-G. Proc. Nat. Acad. Sci. USA. 70: 147–150.
Highland, J. H., Ochsner, E., Gordon, J., Hasenbank, R., and Stöffler, G. 1974. Inhibition of phenylalanyl-tRNA binding and EF-Tu-dependent GTP hydrolysis by antibodies specific for several ribosomal proteins. J. Mol. Biol. 86: 175–178.
Hindley, J., and Page, S. M. 1972. Nucleotide sequence of yeast 5 S rRNA. FEBS Lett. 26: 157–160.
Hindley, J., and Staples, D. H. 1969. Sequence of a ribosome binding site in bacteriophage Q/3-RNA. Nature. 224: 964–967.
Hirashima, A., Wang, S., and Inouye, M. 1974. Cell-free synthesis of a specific lipoprotein of the E. coli. outer membrane directed by purified mRNA. Proc. Nat. Acad. Sci. USA. 71: 4149–4153.
Hirsch, C. A., Cox, M. A., von Venrooij, W. J., and Henshaw, E. C. 1973. The ribosome cycle in mammalian protein synthesis. J. Biol. Chem. 248: 4377–4385.
Hitz, H., Schäfer, D., and Wittmann-Liebold, B. 1975. Primary structure of ribosomal protein S6 from the wild type and a mutant of E. coli. FEBS Lett. 56: 259–262.
Hodge, L. D., Robbins, E., and Scharff, M. D. 1969. Persistence of mRNA through mitosis in HeLa cells. J. Cell Biol. 40: 497–507.
Holland, M. J., Hager, G. L., and Rutter, W. J. 1977. Characterization of purified poly(A)-containing mRNA from S. cerevisiae. Biochemistry. 16: 8–16.
Houdebine, L. M. 1976. Absence of poly(A) in a large part of newly synthesized casein mRNAs. FEBS Leu. 66: 110–113.
Howard, G. A., and Herbert, E. 1975. Ribosomal subunit localization of hemoglobin mRNA. Eur. J. Biochem. 54: 75–80.
Howard, G. A., Traugh, J. A., Croser, E. A., and Traut, R. A. 1975. Ribosomal proteins from rabbit reticulocytes. J. Mol. Biol. 93: 391–404.
Hsu, W. T., and Weiss, S. B. 1969. Selective translation of T4 template RNA by ribosomes from T4-infected E. coli. Proc. Nat. Acad. Sci. USA. 64: 345–351.
Huynh-Van-Tan, Delaunay, J., and Schapira, G. 1971. Eukaryotic ribosomal proteins. FEBS Lett. 17: 163–167.
Iatrou, K., and Dixon, G. H. 1977. The distribution of poly(A)+ and poly(A)- protamine mRNA sequences in the developing trout testis. Cell. 10: 433–441.
Igarashi, K., Sugawara, K., Izumi, I., Nagayama, C., and Hirose, S. 1974. Effect of polyamines on polyphenylalanine synthesis by E. coli. and rat liver ribosomes. Eur. J. Biochem. 48: 495–502.
Ilan, Jo. 1969. The role of tRNA in translational control of specific mRNA during insect metamorphosis. Cold Spring Harb. Symp. Quant. Biol. 34: 787–791.
Ilan, Jo. and Ilan, Ju. 1973a. Sequence homology at the 5’-termini of insect mRNA. Proc. Nat. Acad. Sci. USA. 70: 1355–1358.
Ilan, Ju., and Ilan, Jo. 1973b. An mRNA bound initiation factor and its role in translation of natural message. Nature New Biol. 241: 176–180.
Ilan, Jo., Ilan, Ju., and Quastel, J. H. 1966. Effects of actinomysin D on nucleic acid metabolism and protein biosynthesis during metamorphosis of Tenebrio molitor. L. Biochem. J. 100: 441–447.
Inoue-Yokosawa, N., Ishikawa, C., and Kagiro, Y. 1974. The role of guanosine triphosphate in translocation reaction catalyzed by EF-G. J. Biol. Chem. 249: 4321–4323.
Ishikura, H., Yamada, Y., and Nishimura, S. 1971. Structure of serine tRNA from E. coli. and purification of serine tRNAs with different codon responses. Biochim. Biophys. Acta. 228: 471–481.
Ishizuka, S., Kawakami, M., Ejiri, S., and Shimura, K. 1974. The initiator amino acid in silk fibroin biosynthesis. FEBS Lett. 47: 318–322.
Isono, K., and Isono, S. 1976. Lack of ribosomal protein S1 in Bacillus stearothermophilus. Proc. Nat. Acad. Sci. USA. 73: 767–770.
Isono, S., and Isono, K. 1975. Purification and characterization of 30 S ribosomal proteins from Bacillus stearothermophilus. Eur. J. Biochem. 50: 483–488.
Iwasaki, K., Motoyoshi, K., Nagata, S. and Kaziro, Y. 1976. Purification and properties of a new polypeptide chain elongation factor, EF-1$, from pig liver. J. Biol. Chem. 251: 1843–1845.
Jacob, F., and Monod, J. 1961. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3: 318–356.
Jacobson, A., Firtel, R. A., and Lodish, H. F. 1974. Synthesis of messenger and ribosomal RNA precursors in isolated nuclei of the cellular slime mold Dictyostelium discoideum. J. Mol. Biol. 82: 213–230.
Jantzen, H. 1974. Polyadenylsäure-enthaltende RNA und Genaklivitätsmuster während der Entwicklung von Acanthamoeba castellanü. Biochim. Biophys. Acta. 374: 38–51.
Jay, G., and Kaempfer, R. 1975. Initiation of protein synthesis. Binding of mRNA. J. Biol. Chem. 250: 5742–5748.
Jeffery, W. R., and Brawerman, G. 1974. Characterization of the steady-state population of mes- senger RNA and its poly(A) segment in mammalian cells. Biochemistry. 13: 4633–4637.
Jerez, C., Sandoval, A., Allende, J., Henes, C., and Ofengand, J. 1969. Specificity of the interaction of aminoacyl RNA with a protein-GTP complex from wheat embryo. Biochemistry. 8: 3006–3014.
Johnson, T. C., and Luttges, M. W. 1966. The effects of maturation on in vitro. protein synthesis by mouse brain cells. J. Neurochem. 13: 545–552.
Johnston, R. E., and Bose, H. R. 1972. An adenylate-rich segment in the virion RNA of Sindbis virus. Biochem. Biophys. Res. Comm. 46: 712–718.
Jordan, B. R., and Galling, G. 1973. Nucleotide sequence of Chlorella. cytoplasmic 5 S RNA. FEBS Lett. 37: 333–334.
Jordan, B. R., Galling, G., and Jourdan, R. 1974. Sequence and conformation of 5 S RNA from Chlorella. cytoplasmic ribosomes: Comparison with other 5 S RNA molecules. J. Mol. Biol. 87: 205–225.
Jukes, T. H. 1969. Recent advances in studies of evolutionary relationships between proteins and nucleic acids. Space Life Sci. 1: 469–494.
Kabat, D. 1975. Potentiation of hemoglobin mRNA. J. Biol. Chem. 250: 6085–6092.
Kaempfer, R. 1968. Ribosome subunit exchange during protein synthesis. Proc. Nat. Acad. Sci. USA. 61: 106–113.
Kaempfer, R. 1969. Ribosome subunit exchange in the cytoplasm of a eucaryote. Nature. 222: 950–953.
Kaempfer, R., and Meselson, M. 1968. Permanent association of 5 S RNA molecules with 50 S ribosomal subunits in growing bacteria. J. Mol. Biol. 34: 703–708.
Kaempfer, R., Meselson, M., and Raskas, H. 1968. Cyclic dissociation into stable subunits and reformation of ribosomes during bacterial growth. J. Mol. Biol. 31: 277–289.
Kaji, A., Kaji, H., and Novelli, G. D. 1965. Soluble amino acid-incorporating system. J. Biol. Chem. 240: 1185–1191.
Kaltschmidt, E., Kahan, L., and Nomura, M. 1974. In vitro synthesis of ribosomal proteins directed by E. coli DNA. Proc. Nat. Acad. Sci. USA. 7./:446–450.
Kates, J. 1970. Transcription of the vaccinia virus genome and the occurrence of poly(A) sequences in mRNA. Cold Spring Harbor Symp. Quant. Biol. 35: 743–752.
Kawakita, M., Arai, K.-I., and Kaziro, Y. 1974. Interactions between EF-Tu-guanosine triphosphate and ribosomes and the role of ribosome-bound tRNA in guanosine triphosphate reaction. J. Biochem. 76: 801–809.
Kay, A., Sander, G., and Grunberg-Manago, M. 1973. Effect of ribosomal protein L12 upon initiation factor IF-2 activities. Biochem. Biophys. Res. Comm. 51: 979–986.
Kaziro, Y., Inoue-Yokosawa, N., and Kawakita, M. 1972. Studies on polypeptide EF-G from E. coli. J. Biochem. 72: 853–863.
Kemp, D. J. 1975. Unique and repetitive sequences in multiple genes for feather keratin. Nature. 254: 573–575.
Kim, S.-H., and Rich, A. 1969. Crystalline transfer RNA: The three-dimensional Patterson function of 12-Angstrom resolution. Science. 166: 1621–1624.
Kim, W. S. 1969. N-formylseryl-tRNA. Science. 163: 947–949.
Kimura, M., and Ohta, T. 1973. Eukaryotes-prokaryotes divergence estimated by 5 S ribosomal RNA sequences. Nature New Biol. 243: 199–200.
Kischa, K., Möller, W., and Stöffler, G. 1971. Reconstitution of a GTPase activity by a 50 S ribosomal protein from E. coli. Nature New Biol. 233: 62–63.
Kiselev, N. A., Stel’mashchuk, V. Y., Lerman, M. I., and Abakumova, O. Y. 1974. On the structure of liver ribosomes. J. Mol. Biol. 86: 577–586.
Kiss, A., Sain, B., and Venetianer, P. 1977. The number of rRNA genes in E. coli. FEBS Lett. 79: 77–79.
Klagsbrun, M. 1973. An evolutionary study of the methylation of tRNA and rRNA in prokaryote and eukaryote organisms. J. Biol. Chem. 248: 2612–2620.
Klein, W. H., Murphy, W., Attardi, G., Britten, R. J., and Davidson, E. H. 1974. Distribution of repetitive and nonrepetitive sequence transcripts in HeLa mRNA. Proc. Nat. Acad. Sci. USA. 71: 1785–1789.
Knight, E. J. R., and Darnell, J. E. 1967. Distribution of 5 S RNA in HeLa cells. J. Mol. Biol. 28: 491–502.
Kohler, R. E., Ron, E. Z., and Davis, B. D. 1968. Significance of the free 70S ribosomes in E. coli. extracts. J. Mol. Biol. 36: 71–82.
Kolakofsky, D., Dewey, K., and Thack, R. E. 1969. Purification and properties of initiation factor f2. Nature. 223: 694–697.
Koser, R. B., and Collier, J. R. 1971. The molecular weight and thermolability of Ilyanassa. •rRNA. Biochim. Biophys. Acta. 254: 272–277.
Koteliansky, V. E., Domogatsky, S. P., Gudkov, A. T., and Spirin, A. S. 1977. Elongation factor-dependent reactions on ribosomes deprived of proteins L7 and L12. FEBS Lett. 73: 6–11.
Krauss, S. W., and Leder, P. 1975. Turnover of protein synthetic elongation and initiation factors in E. coli. J. Biol. Chem. 250: 4714–4717.
Krystosek, A., Cawthon, M. L., and Kabat, D. 1975. Improved methods for purification and assay of eukaryotic mRNAs and ribosomes. J. Biol. Chem. 250: 6077–6084.
Küntzel, H. 1969. Proteins of mitochondria) and cytoplasmic ribosomes. Nature. 222: 142–146.
Kurland, C. G. 1970. Ribosome structure and function emergent. Science. 169: 1171–1177.
Kwan, S. W., and Brawerman, G. 1972. A particle associated with the poly(A) segment in mammalian mRNA. Proc. Nat. Acad. Sci. USA. 69: 3247–3250.
Lai, M. M. C., and Duesberg, P. H. 1972. Adenylic acid-rich sequence in RNA of Rous sarcoma virus and Rausche mouse leukaemia virus. Nature. 235: 383–386.
Lake, J. A. 1976. Ribosome structure determined by electron microscopy of E. coli. small subunits, large subunits and monomeric ribosomes. J. Mol. Biol. 105: 131–159.
Lanzani, G. A., Bollini, R., and Soffientini, A. N. 1974. Heterogeneity of EF-1 from wheat embryos. Biochim. Biophys. Acta. 335: 275–283.
Lawrence, F. 1973. Effect of adenosine on methionyl-tRNA synthetase. Eur. J. Biochem. 40: 493–500.
Lawrence, F., Blanquet, S., Poiret, M., Robert-Gero, M., and Waller, J.-P. 1973. The mechanism of action of methionyl-tRNA synthetase. Eur. J. Biochem. 36: 234–243.
Lawrence, F., Shire, D. J., and Waller, J.-P. 1974. The effect of adenosine analogues on ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase. Eur. J. Biochem. 41: 73–81.
Laycock, A. G., and Hunt, J. A. 1969. Synthesis of rabbit globin by a bacterial cell-free system. Nature. 221: 1118–1122.
Leaver, C. J., and Ingle, J. 1971. The molecular integrity of chloroplast rRNA. Biochem. J. 123: 235–243.
LeBleu, B., Nudel, U., Falcoff, E., Prives, C., and Revel, M. 1972. A comparison of the translation of Mengo virus RNA and globin mRNA in Krebs ascites cell-free extracts. FEBS Lett. 25: 97–103.
Lebleu, G., Marbaix, G., Huez, G., Timmerman, J., Burny, A., and Chantrenne, N. 1971. Characterization of the mRNP released from reticulocyte polyribosomes by EDTA treatment. Eur. J. Biochem. 19: 264–269.
Leder, P. 1973. The elongation factors in protein synthesis. Adv. Prot. Chem. 27: 213–240.
Lee-Huang, S., and Ochoa, S. 1973. Purification of two messenger-discriminating species of IF-3 from E. coli. Methods Enzymol. 30: 45–53.
Lee-Huang, S., and Ochoa, S. 1974a. Preparation and properties of crystalline initiation factor 1 (IFI) from Escherichia coli. Methods Enzymol. 30: 31–39.
Lee-Huang, S., and Ochoa, S. 1974b. Pruification of two messenger-discriminating species of initiation factor 3 (IF3) from E. coli. Methods Enzymol. 30: 45–53.
Leffler, S. and Szer, W. 1974a. Purification and properties of initiation factor IF-3 from Caulobacter crescentus. J. Biol. Chem. 249: 1458–1464.
Leffler, S., and Szer, W. 1974b. Polypeptide chain initiation in Caulobacter crescentus. without initiation factor IF-1. J. Biol. Chem. 249: 1465–1468.
Leibowitz, M. J., and Soffer, R. L. 1969. A soluble enzyme from E. coli. which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins. Biochem. Biophys. Res. Comm. 36: 47–53.
Leighton, T. 1974. Further studies on the stability of sporulation mRNA in B. subtilis. J. Biol. Chem. 249: 7808–7812.
Levin, D. H., Kyner, D., and Acs, G. 1973. Protein initiation in eukaryotes. Proc. Nat. Acad. Sci. USA. 70: 41–45.
Levinthal, C., Hosoda, J., and Shub, D. 1967. The control of protein synthesis after phage infection. In: Colter, S. J., and W. Paranchych, eds., The Molecular Biology of Viruses., New York, Academic Press, p. 71–87.
Levinthal, C., Keywan, A., and Higa, A. 1962. Messenger RNA turnover and protein synthesis in B. subtilis. inhibited by actinomycin D. Proc. Nat. Acad. Sci. USA. 48: 1631–1638.
Levitt, M. 1969. Detailed molecular model for tRNA. Nature. 224: 759–763.
Lewin, B. M. 1970. The Molecular Basis of Gene Expression. New York, Wiley-Interscience.
Liautard, J. P., Setyono, B., Spindler, E., and Köhler, K. 1976. Comparison of proteins bound to the different functional classes of mRNA. Biochim. Biophys. Acta. 425: 373–383.
Lim, L., and Canellakis, E. S. 1970. Adenine-rich polymer associated with rabbit reticulocyte mRNA. Nature. 227: 710–712.
Lim, L., Canellakis, Z. N. and Canellakis, E. S. 1970. Metabolism of naturally occurring homo-polymers. Biochim. Biophys. Acta. 209: 128–138.
Lin, J. Y., Tsung, C. M., and Fraenkel-Conrat, J. 1967. The coat protein of the RNA bacteriophage MS2. J. Mol. Biol. 24: 1–14.
Lipmann, F. 1969. Polypeptide chain elongation in protein biosynthesis. Science. 164: 1024–1031.
Loeb, J. N., Howell, R. R., and Tomkins, G. M. 1965. Turnover of rRNA in rat liver. Science. 149: 1093–1095.
Loening, U. E. 1968. Molecular weights of rRNA in relation to evolution. J. Mol. Biol. 38: 355–365.
Loening, U. E., Grierson, D., Rogers, M. E., and Sartirana, M. L. 1972. Properties of rRNA precursor. In: Cox, R. A., and A. A. Hadjiolov, eds., Functional Units in Protein Biosynthesis., New York, Academic Press, p. 395–405.
Loftfield, R. B. 1972. The mechanism of aminoacylation of tRNA. Progr. Nucl. Acid. Res. Mol. Biol. 12: 87–128.
Lucas-Lenard, J., and Lipmann, F. 1966. Separation of three microbial amino acid polymerization factors. Proc. Nat. Acad. Sci. USA. 55: 1562–1566.
Lucas-Lenard, J., and Lipmann, F. 1971. Protein biosynthesis. Ann. Rev. Biochem. 40: 409–448.
Lukanidin, E. M., Zalmanzon, E. S., Komaromi, L., Samarina, O. P., and Georgiev, G. P. 1972. Structure and function of informofers. Nature New Biol. 238: 193–197.
Maclnnes, J. W. 1972. Differences between ribosomal subunits from brain and those from other tissues. J. Mol. Biol. 65: 157–162.
Maclnnes, J. W. 1973. Mammalian brain ribosomes are behaviourly and structurally heterogeneous. Nature New Biol. 241: 244–246.
MacLeod, M. C. 1975. Comparisons of the properties of cytoplasmic poly(A)-containing RNA from polysomal and nonpolysomal fractions of murine myeloma cells. Biochemistry. 14: 4011–4018.
Maden, B. E. H., Forbes, J., de Jong, P., and Klootwijk, J. 1975. Presence of a hypermodified nucleotide in HeLa cell 18 S and Saccharomyces carlsbergensis. 17. S ribosomal RNAs. FEBS Lett. 59: 60–63.
Madison, J. T. 1968. Primary structure of RNA. Ann. Rev. Biochem. 37: 131–148.
Maelicke, A., Engel, G., Cramer, F., and Staehelin, M. 1974. ATP-induced specificity of the binding of serine tRNAs from rat liver to seryl-tRNA sythetase from yeast. Eur. J. Biochem. 42: 311–314.
Mainwaring, W. I. P., Wilce, P. A., and Smith, A. E. 1974. Studies on the form and synthesis of mRNA in the rat ventral prostate gland, including its tissue-specific stimulation by androgens. Biochem. J. 137: 513–524.
Maizels, N. 1974. E. coli. lactose operon ribosome binding site. Nature. 249: 647–649.
Majumdar, A., Bose, K. K., and Gupta, N. K. 1976. Specific binding of E. coli. chain IF-2 to fMet-tRNA r r. J. Biol. Chem. 251: 137–140.
Mangiarotti, G., and Schlessinger, D. 1966. Extraction of polyribosomes and ribosomal subunits from fragile growing E. coli. J. Mol. Biol. 20: 123–143.
Mangiarotti, G., and Schlessinger, D. 1967. Formation and lifetime of mRNA molecules, ribosome subunit couples and polyribosomes. J. Mol. Biol. 29: 355–418.
Mansbridge, J. N., Crossley, J. A., Lanyon, W. G., and Williamson, R. 1974. The poly(A) sequence of mouse globin mRNA. Eur. J. Biochem. 44: 261–269.
Marcus, A., Seal, S. N., and Weeks, D. P. 1974. Protein chain initiation in wheat embryo. Methods Enzymol. 30: 94–101.
Marshall, R. E. 1967. Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA. Science. 155: 820–826.
Mathews, M. B., Osburn, M., Berns, A. J. M., and Bloemandal, H. 1972a. Translation of two mRNAs from lens in a cell-free system from Krebs II ascites cells. Nature New Biol. 236: 5–7.
Mathews, M. B., Pragnell, I. B., Osburn, M., and Arnstein, H. R. V. 1972b. Stimulation by reticulocyte initiation factors of protein synthesis in a cell-free system from Krebs II ascites cells. Biochim. Biophys. Acta. 287: 113–123.
Maugh, T. H. 1975. Ribosomes (II): A complicated structure begins to emerge. Science. 190: 258–260.
Mazumder, R. 1971. Studies on polypeptide chain initiation factors F, and F2. FEBS Lett. 18: 64–66.
Mazumder, R. 1972. IF-2-dependent ribosomal binding ofN-formylmethionyl-tRNA without added GTP. Proc. Nat. Acad. Sci. USA. 69: 2770–2773.
McConkey, E. H., and Hauber, E. J. 1975. Evidence for heterogeneity of ribosomes within the HeLa cell. J. Biol. Chem. 250: 1311–1318.
McCorquodale, D. J., Oleson, A. E., and Buchanan, J. M. 1967. Control of virus-induced enzyme synthesis in bacteria. In: Colter, S. J., and W. Paranchych, eds., The Molecular Biology of Viruses., New York, Academic Press, p. 31–54.
McCroskey, R. P., Zasloff, M., and Ochoa, S. 1972. Polypeptide chain initiation and stepwise elongation with Artemia. ribosomes and factors. Proc. Nat. Acad. Sci. USA. 69: 2451–2455.
McKnight, G. S., and Schimke, R. T. 1974. Ovalbumin mRNA. Proc. Nat. Acad. Sci. USA. 71: 4327–4331.
McLaughlin, C. S., Warner, J. R., Edmunds, M., Nakagato, H., and Vaughan, M. H. 1973. Poly(A) sequences in yeast mRNA. J. Biol. Chem. 248: 1466–1471.
McNeil, R. G., and McLaughlin, C. S. 1974. Differential biological activity of three species of methionyl-tRNA in yeast. Biochim. Biophys. Acta. 374: 176–186.
Meier, D., Lee-Huang, S., and Ochoa, S. 1973. Factor requirements for initiation complex formation with natural and synthetic messengers in E. coli. systems. J. Biol. Chem. 248: 8613–8615.
Merkel, C. G., Wood, T. G., and Lingal, J. B. 1976. Shortening of the poly(A) region of mouse globin mRNA. J. Biol. Chem. 251: 5512–5515.
Mertes, M., Peters, M. A., Mahoney, W., and Yarus, M. 1972. Isoleucylation of tRNAFet (E. coli). by isoleucyl-tRNA synthetase from E. coli. J. Mol. Biol. 71: 671–685.
Mescher, A., and Humphreys, T. 1974. Activation of maternal mRNA in the absence of poly(A) formation in fertilised sea urchin eggs. Nature. 249: 138–139.
Metafora, S., Terada, M., Dow, L. W., Marks, P. A., and Bank, A. 1972. Increased efficiency of exogenous mRNA translation in a Krebs ascites cell lystate. Proc. Nat. Acad. Sci. USA. 69: 1299–1303.
Meyer, M., Bout, W. S., de Vries, M., and Nanninga, N. 1974. Electron microscopic and sedimentation studies on rat-liver ribosomal subunits. Eur. J. Biochem. 42: 259–268.
Miller, D. L., and Weissbach, H. 1974. Elongation factor Tu and the aminoacyl-tRNA EF-Tu GTP complex. Methods Enzymol. 30: 219–232.
Miller, R. V., and Sypherd, P. S. 1973. Topography of the E. coli. 30 S ribosome revealed by the modification of ribosomal proteins. J. Mol. Biol. 78: 539–550.
Milman, G., Goldstein, J., Scolnick, E., and Caskey, T. 1969. Peptide chain termination. Proc. Nat. Acad. Sci. USA. 63: 183–190.
Min Jou; W., Haegeman, G., Ysebaert, M., and Fiers, W. 1972. Nucleotide sequence of the gene. coding for the bacteriophage MS2 coat protein. Nature. 237: 82–88.
Miyazaki, M. 1974. Studies on the nucleotide sequence of pseudoruidine-containing 5 S RNA from S. cerevisiae. J. Biochem. 75: 1407–1410.
Mizumoto, K., Iwasaki, K. Kazior, Y., Nojiri, C., and Yamada, Y. 1974. Studies on peptide EF-2 from pig liver. J. Biochem. 75: 1057–1062.
Modolell, J. 1974. The initial steps in protein synthesis. Methods Enzymol. 30: 79–86.
Monroy, A., Maggio, R., and Rinaldi, A. M. 1965. Experimentally induced activation of the ribosomes of the unfertilized sea urchin egg. Proc. Nat. Acad. Sci. USA. 54: 107–111.
Montagnier, L., Collandre, H., De Maeyer-Guiguard, J., and De Maeyer, E. 1974. Two forms of mouse interferon mRNA. Biochem. Biophys. Res. Comm. 59: 1031–1038.
Moore, P. B., Engelman, D. M., and Schoenborn, B. P. 1974. Asymmetry in the 50 S ribosomal subunit of E. coli. Proc. Nat. Acad. Sci. USA. 71: 172–176.
Moore, V. G., Atchison, R. E., Thomas, G., Moran, M., and Noller, H. F., 1975. Identification of a ribosomal protein essential for peptidyl transferase activity. Proc. Nat. Acad. Sci. USA. 72: 844–848.
Morel, C., Kayibanda, B. and Scherrer, K. 1971. Proteins associated with globin mRNA in avian erythroblasts. FEBS Lett. 18: 84–88.
Morell, P., and Marmur, J. 1968. Association of 5 S RNA to 50 S subunits of E. coli. and B. subtilis. Biochemistry. 7: 1141–1152.
Morikawa, N., and Imamoto, F. 1969. On the degradation of mRNA for the tryptophan operon in E. coli. Nature. 223: 37–40.
Morinaga, T., Funatsu, G., Funatsu, M., and Wittmann, H. G. 1976. Primary structure of the 16 S rRNA binding protein Sl5 from E. coli. ribosomes. FEBS Lett. 64: 307–309.
Munsche, D., and Wollgiehn, R. 1974. Altersabhängige labilität der ribosomalen RNA aus chloroplasten von Nicotiana rustica. Biochim. Biophys. Acta. 340: 437–445.
Murthy, M. R. V. 1972. Free and membrane bound ribosomes of rat cerebral cortex. J. Biol. Chem. 247: 1936–1943.
Musso, R. E., de Crombrugghe, B., Pastan, I., Sklar, J., Yot, P., and Weissman, S. 1974. The 5’-terminal nucleotide sequence of galactose mRNA of E. coli. Proc. Nat. Acad. Sci. USA. 71: 4941–4944.
Muthukrishnan, S., Both, G. W., Furuichi, Y., and Shatkin, A. J. 1975. 5’-terminal 7-methylguanosine in eukaryotic mRNA is required for translation. Nature. 255: 33–37.
Muto, A. 1970. Nucleotide distribution of E. coli. 16 S rRNA. Biochemistry. 9: 3683–3693.
Naaktgeboren, N., Roobol, K., and Voorma, H. O. 1977. The effect of the initiation factor IF-1 on the dissociation of 70-S ribosomes of E. coli. Eur. J. Biochem. 72: 49–56.
Nakamoto, T., Conway, T. W., Allende, J. E., Spyrides, G. J., and Lipmann, F. 1963. Formation of peptide bonds. Cold Spring Harbor Symp. Quant. Biol. 28: 227–232.
Nakazato, H., Venkatesan, S., and Edmonds, M. 1975. Poly(A) sequences in E. coli. mRNA. Nature. 256: 144–146.
Nanninga, A. 1973. Structural aspects of ribosomes. Int. Rev. Cytol. 35: 135–188.
Natale, P. J., and Buchanan, J. M. 1974. Initiation characteristics for the synthesis of five T4 phage-specific mRNAs in vitro. Proc. Nat. Acad. Sci. USA. 71: 422–426.
Nathans, D., and Lipmann, F. 1961. Amino acid transfer from aminoacyl-RNAs to protein on ribosomes of E. coli. Proc. Nat. Acad. Sci. USA. 47: 497–504.
Nazar, R. N., Sitz, T. O., and Busch, H. 1975. Tissue specific differences in the 2’-O-methylation of eukaryotic 5.8 S ribosomal RNA. FEBS Lett. 59: 83–87.
Nazar, R. N., Sitz, T. O., and Busch, H. 1976. Sequence homologies in mammalian 5.8 S rRNA. Biochemistry. 15: 505–508.
Nesbitt, J. A., and Lennarz, W. J. 1968. Participation of aminoacyl tRNA in aminoacyl phosphatidylglycerol synthesis. J. Biol. Chem. 243: 3088–3095.
Nishikawa, K., and Takemura, S. 1974. Nucleotide sequence of 5 S RNA from Torulopsis utilis. FEBS Lett. 40: 106–109.
Nishizuka, Y., and Lipmann, F. 1966. Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli. system. Proc. Nat. Acad. Sci. USA. 55: 212–219.
Nolan, R. D., Grasmuk, H., Högenauer, G., and Drews, J. 1974. EF-1 from Krebs II mouse ascites cells. Eur. J. Biochem. 45: 601–609.
Nolan, R. D., Grasmuk, H., and Drews, J. 1975. The binding of tritiated EF-1 and EF-2 to ribosomes from Krebs II mouse ascites tumor cells. Eur. J. Biochem. 50: 391–402.
Noller, H. F. 1974. Topography of 16 S RNA in 30 S ribosomal subunits. Biochemistry. 13: 4694–4703.
Noller, H. F., and Herr, W. 1974. Nucleotide sequence of the 3’-terminus of E. coli. 16 S rRNA. Mol. Biol. Repts. 1: 437–439.
Nomura, M. 1973. Assembly of bacterial ribosomes. Science. 179: 864–873.
Nudel, U., LeBleu, B., Zehavi-Willner, T., and Revel, M. 1973. Messenger RNP and initiation factors in rabbit-reticulocyte polyribosomes. Eur. J. Biochem. 33: 314–322.
Ohta, N., Sanders, M., and Newton, A. 1975. Poly(A) sequences in the RNA of Caulobacter crescentus. Proc. Nat. Acad. Sci. USA. 72: 2343–2346.
Olsnes, S. 1970. Characterization of protein bound to rapidly-labeled RNA in polyribosomes from rat liver. Eur. J. Biochem. 15: 464–471.
Ono, Y., Skoultchi, A., Klein, A.; and Lengyel, P. 1968. Discrimination against the initiator tRNA by microbial amino-acid polymerization factors. Nature. 220: 1304–1307.
Otaka, T., and Kaji, A. 1974. Inhibitory effect of EF-G and GMPPCP on peptidyl transferase. FEBS Lett. 44: 324–329.
Ouellette, A. J., and Malt, R. A. 1976. Accumulation and decay of mRNA in mouse kidney. Biochemistry. 15: 3358–3361.
Pace, N. R. 1973. Structure and synthesis of the rRNA of prokaryotes. Bact. Rev. 37: 562–603.
Pace, N. R., Walker, T. A., and Pace, B. 1974. The nucleotide sequence of chicken 5 S rRNA. J. Mol. Evol. 3: 151–159.
Pain, V. N., and Clemens, M. J. 1973. The role of soluble protein factors in the translational control of protein synthesis in eukaryotic cells. FEBS Lett. 32: 205–212.
Paradies, H. H., Franz, A., Pon, C. L., and Gualerzi, C. 1974. Conformational transition of the 30 S ribosomal subunit induced by IF-3. Biochem. Biophys. Res. Comm. 59: 600–607.
Payne, P. I., Woledge, J., and Cony, M. J., 1973. No evidence for tissue-specific sequences of cytoplasmic 5 S and 5.8 S ribosomal RNAs in the broad bean. FEBS Lett. 35: 327–330.
Peeters, B., Vanduffel, L., Depuydt, A., and Rombauts, W. 1973. The number and size of the proteins in the subunits of human placental ribosomes. FEBS Lett. 36: 217–221.
Pemberton, R. E., Housman, D., Lodish, H., and Baglioni, C. 1972. Isolation of duck haemoglobin mRNA and its translation by rabbit reticulocyte cell-free system. Nature New Biol. 235: 99–102.
Pene, J. J., Knight, E., and Darnell, J. E. 1968. Characterization of a new low molecular weight RNA in HeLa cell ribosomes. J. Mol. Biol. 33: 609–624.
Penman, S., Scherrer, K., Becker, Y., and Darnell, J. E. 1963. Polyribosomes in normal and poliovirus infected HeLa cells and their relationship to mRNA. Proc. Nat. Acad. Sci. USA. 49: 654–662.
Perlman, S., Abelson, H., and Penman, S. 1973. Mitochondrial protein synthesis: RNA with the properties of eukaryotic mRNA. Proc. Nat. Acad. Sci. USA. 70: 350–353.
Perlman, S., Hirsch, M., and Penman, S. 1972. Utilization of messenger in adenovirus-2-infected cells at normal and elevated temperatures. Nature New Biol. 238: 143–144.
Perry, R. P., and Kelley, D. E. 1974. Existence of methylated mRNA in mouse L cells. Cell. I: 37–42.
Perry, R. P., Kelley, D. E., and La Torre, J. 1972. Lack of poly(A) sequences in the mRNA of E. coli. Biochem. Biophys. Res. Comm. 48: 1593–1600.
Perry, R. P., and Scherrer, K. 1975. The methylated constituents of globin mRNA. FEBS Lett. 57: 73–78.
Person, S., and Osburn, M. 1968. The conversion of amber. suppressors to ochre. suppressors. Proc. Nat. Acad. Sci. USA. 60: 1030–1038.
Petersen, N. S., and McLaughlin, C. S. 1973. Monocistronic mRNA in yeast. J. Mol. Biol. 81: 33–45.
Petrissant, G. 1973. Evidence for the absence of the G-T-/t-C sequence from two mammalian initiator transfer RNAs. Proc. Nat. Acad. Sci. USA. 70: 1046–1049.
Philipson, L., Wall, R., Glickman, G., and Darnell, J. E. 1971. Addition of poly(A) sequences to virus-specific RNA during adenovirus replication. Proc. Nat. Acad. Sci. USA. 68: 2806–2809.
Pieczenik, G., Horiuchi, K., Model, P., McGill, C., Mazur, B. J., Vorts, G. F., and Zinder, N. D. 1975. Is mRNA transcribed from the strand complementary to it in a DNA duplex? Nature. 253: 131–132.
Polya, G. M., and Phillips, D. R. 1976. The occurrence in amino acid sequences of extensive informational symmetries based on possible codon-codon complementarity in the encoding polynucleotides. Biochem. J. 153: 681–690.
Pribula, C. D., Fox, G. E., and Woese, C. R. 1974. Nucleotide sequence of Bacillus megaterium. 5 S RNA. FEBS Lett. 44: 322–323.
Pribula, C. D., Fox, G. E., and Woese, C. R. 1976. Nucleotide sequence of Clostridium pasteurianum. 5. S rRNA. FEBS Lett. 64: 350–352.
Procunier, J. D., and Tartof, K. D. 1976. Restriction map of 5 S RNA genes of D. melanogaster. Nature. 263: 255–257.
Puckett, L., Chambers, S., and Darnell, J. E. 1975. Short-lived mRNA in HeLa cells and its impact on the kinetics of accumulation of cytoplasmic polyadenylate. Proc. Nat. Acad. Sci. USA. 72: 389–393.
Rawson, J. R., and Stutz, E. 1968. Characterization of Euglena. cytoplasmic ribosomes and rRNA by zone velocity sedimentation in sucrose gradients. J. Mol. Biol. 33: 309–314.
Reid, B. R., Einarson, B., and Schmidt, J. 1972. Loop accessibility in transfer RNA. Biochimie. 54: 325–332.
Reinbolt, J., and Schiltz, E. 1973. The primary structure of ribosomal protein S4 from E. coli. FEBS Lett. 36: 250–252.
Retel, J., and Planta, R. J. 1968. Investigation of the rRNA sites in yeast DNA by the hybridization technique. Biochim. Biophys. Acta. 169: 416–429.
Revel, M., Lelong, J. C., Brawerman, G., and Gros, F. 1968a. Function of three protein factors and ribosomal subunits in the initiation of protein synthesis in E. coli. Nature. 219: 1016 1020.
Revel, M., Herzberg, H., Becarevic, A., and Gros, F. 1968b. Role of a protein factor in the functional binding of ribosomes to natural mRNA. J. Mol. Biol. 33: 231–249.
Rho, H. M., and Green, M. 1974. The homopolyadenylate and adjacent nucleotides at the 3’-terminus of 30–40 S RNA subunits in the genome of murine sarcoma-leukemia virus. Proc. Nat. Acad. Sci. USA. 71: 2386–2390.
Ricard, B., and Salser, W. 1974. Size and folding of the messenger for phage T4 lysozyme. Nature. 248: 314–317.
Ricard, B., and Salser, W. 1975. Secondary structures formed by random RNA sequences. Biochem. Biophys. Res. Comm. 63: 548–554.
Richter, D., Erdmann, V. A., and Sprinzl, M. 1973. Specific recognition of GTiiC loop (Loop IV) of tRNA by 50 S ribosomal subunits. Nature New Biol. 246: 132–135.
Riley, W. T. 1973. Amino acid sequences and double-stranded messages-a means of directing the site of mutation? J. Theor. Biol. 40: 285–300.
Ringer, D., and Chlâdek, S. 1974. Ribosomal peptidyl transferase: recognition points on the 3’-terminus of AA-tRNA. FEBS Lett. 39: 75–78.
Ritter, E., and Wittmann-Liebold, B. 1975. The primary structure of protein L30 from E. coli. ribosomes. FEBS Lett. 60: 153–155.
Roberts, R. J. 1972. Structure of two glycyl-tRNAs from Staphylococcus epidermidis. Nature New Biol. 237: 44–45.
Robinson, E. A., Henriksen, O., and Maxwell, E. S. 1974. Elongation factor 2. J. Biol. Chem. 249: 5088–5093.
Rohrbach, M. S., Dempsey, M. E., and Bodley, J. W. 1974. Preparation of homogeneous EF-G and examination of the mechanism of guanosine triphosphate hydrolysis. J. Biol. Chem. 249: 5094–5101.
Ron, E. Z., Kohler, R. E., and Davis, B. D. 1968. Magnesium ion dependence of free and polysomal ribosomes from E. coli. J. Mol. Biol. 36: 83–90.
Rosbash, M., and Ford, P. J. 1974. Poly(A)-containing RNA in Xenopus laevis. J. Mol. Biol. 85: 87–101.
Rosen, J M., Woo, S. L. C., Holder, J W., Means, A. R., and O’Malley, B. W. 1975. Preparation and preliminary characterization of purified ovalbumin mRNA from the hen oviduct. Biochemistry. 14:69–78.
Rubin, G. M. 1973. The nucleotide sequence of S. cerevisiae. 5.8 S rRNA. J. Biol. Chem. 248: 3860–3875.
Rubin, G. M. 1974. Three forms of the 5.8 S ribosomal RNA species in S. cerevisiae. Eur. J. Biochem. 41: 197–202.
Sabol, S., and Ochoa, S. 1974. Preparation of radioactive IF-3. Methods Enzymol. 30:39–53. Sabol, S., Sillero, M. A. G., Iwasaki, K. and Ochoa, S. 1970. Purification and properties of IF-3. Nature. 228: 1269–1273.
Sadowski, P. D., and Howden, J. A. 1968. Isolation of two distinct classes of polysomes from a nuclear fraction of rat liver. J. Cell. Biol. 37: 163–181.
Sager, R., and M. G. Hutchinson. 1967. Cytoplasmic and chloroplast ribosomes of Chlamydomonas. Science. 157: 709–711.
Sagher, D., Edelman, M., and Jakob, K. M. 1974. Poly(A)-associated RNA in plants. Biochim. Biophys. Acta. 349: 32–38.
Sampson, J., Mathews, M. B., Osburn, M., and Borghetti, A. F. 1972. Hemoglobin mRNA translation in cell-free systems from rat and mouse liver and Landschutz ascites cells. Biochemistry. 11. :3636–3640.
Sanger, F. 1971. Nucleotide sequences in bacteriophage RNA. Biochem. J. 124: 833–843.
Sankoff, D., Morel, C., and Cedergren, R. J. 1973. Evolution of 5 S RNA and the nonrandomness of base replacement. Nature New Biol. 245: 232–234.
Santi, D. V., and Danenberg, P. V. 1971. Phenylalanyl tRNA synthetase from E. coli. Analysis of the phenylalanine binding site. Biochemistry. 10: 4813–4820.
Santi, D. V., Danenberg, P. V., and Satterly, P. 1971. Phenylalanyl tRNA synthetase from E. coli. Reaction parameters and order of substrate addition. Biochemistry. 10: 4804–4812.
Scharff, M. D., and Robbins, E. 1966. Polyribosome disaggregation during metaphase. Science. 151: 922–995.
Schedl, P. D., Singer, R. E., and Conway, T. W. 1970. A factor required for the translation of bacteriophage f2 RNA in extracts of T4-infected cells. Biochem. Biophys. Res. Comm. 38: 631–637.
Schiff, N., Miller, M. J. and Wahba, A. J. 1974. Purification and properties of chain IF-3 from T4-infected and uninfected E. coli. MRE600. J. Biol. Chem. 249: 3797–3802.
Schutz,l E., and Reinbolt, J. 1975. Determination of the complete amino-acid sequence of protein S4 from E. coli. ribosomes. Eur. J. Biochem. 56: 467–481.
Shimotohno, K., Kodama, Y., Hashimoto, J., and Miura, K. 1977. Importance of 5’-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis. Proc. Nat. Acad. Sci. USA. 74: 2734–2738.
Schlessinger, D., Marchesi, V. T., and Kwan, B. C. K. 1965. Binding of ribosomes to cytoplasmic reticulum of Bacillus megaterium. J. Bact. 90: 456–466.
Schrier, P. I., Maassen, J. A., and Möller, W. 1973., Involvement of 50 S ribosomal proteins L6 and L10 in the ribosome dependent GTPase activity of EF-G. Biochem. Biophys. Res. Comm. 53: 90–98.
Schrier, P. I., and Möller, W. 1975. The involvement of 50 S ribosomal protein L11 in the EF-G dependent GTP hydrolysis of E. coli. ribosomes. FEBS Lett. 54: 130–134.
Scolnick, E., Tompkins, R., Caskey, T., and Nirenberg, M. 1968. Release factors differing in specificity for terminator codons. Proc. Nat. Acad. Sci. USA. 61: 768–774.
Seal, S. N., and Marcus, A. 1973. Translation of the initial codons of satellite tobacco necrosis virus RNA in a cell-free system from wheat embryo. J. Biol. Chem. 248: 6577–6582.
Shine, J., and Dalgarno, L. 1973. Occurrence of heat-dissociable rRNA in insects. J. Mol. Biol. 75: 57–72.
Shine, J., and Dalgarno, L. 1974a. The 3’-terminal sequence of E. coli. 16 S ribosomal RNA. Proc. Nat. Acad. Sci. USA. 71: 1342–1346.
Shine, J., and Dalgarno, L. 1974b. Identical 3’-terminal octanucleotide sequence in 18 S ribosomal ribonucleic acid from different eukaryotes. Biochem. J. 141: 609–615.
Shine, J., and Dalgarno, L. 1975. Determinant of cistron specificity in bacterial ribosomes. Nature. 254: 34–38.
Shine, J., Hunt, J. A., and Dalgarno, L. 1974. Studies on the 3’-terminal sequences of the large rRNA of different eukaryotes and those associated with `hidden’ breaks in heat-dissociable insect 26 S RNA. Biochem. J. 141: 617–625.
Siddiqui, M. A. Q., and Hosokawa, N. 1968. Role of 5 S rRNA in polypeptide synthesis. Biochem. Biophys. Res. Comm. 32: 1–8.
Siegert, W., Bauer, G., and Hofschneider, P. H. 1973. Direct evidence for messenger activity of influenza virion RNA. Proc. Nat. Acad. Sci. USA. 70: 2960–2963.
Simsek, M., Petrissant, G., and Rajbhandary, U. L. 1973a. Replacement of the sequence G-T-a(rC-G(A) by G-A-U-C-G in initiator transfer RNA of rabbit liver cytoplasm. Proc. Nat. Acad. Sci. USA. 70: 2600–2604.
Simsek, M., Ziegenmeyer, J., Heckman, J., and Rjbhandary, U. L. 1973b. Absence of the sequence G-T-ijr-C-G(A) in several eukaryotic cytoplasmic initiator transfer RNAs. Proc. Nat. Acad. Sci. USA. 70: 1041–1045.
Singer, R. E., and Conway, T. W. 1973. Defective initiation of f2 RNA translation by ribosomes from bacteriophage T4-infected cells. Biochim. Biophys. Acta. 331: 102–116.
Skogerson, L., and Wakatama, E. 1976. A ribosome-dependent GTPase from yeast distinct from EF-2. Proc. Nat. Acad. Sci. USA. 73: 73–76.
Slack, J. M. W., and Loening, U. E. 1974. 28 S RNA from Xenopus laevis. contains a sequence of three adjacent 2’-O-methylations. Eur. J. Biochem. 43: 69–72.
Slater, I., Gillespie, D., and Slater, D. W. 1973. Cytoplasmic adenylation and processing of maternal RNA. Proc. Nat. Acad. Sci. USA. 70: 406–411.
Slayter, H., Kiho, Y., Hall, C. E., and Rich, A. 1968. An electron microscopic study of large bacterial polyribosomes. J. Cell Biol. 37: 583–590.
Smith, I., Dubnau, D., Morrell, P., and Marmur, J. 1968. Chromosomal location of DNA base sequences complementary to tRNA and to 5 S, 16 S, and 23 S ribosomal RNA in B. subtilis. J. Mol. Biol. 33: 123–140.
Smith, K. E., and Henshaw, E. C. 1975. Binding of met-tRNAf to native and derived 40 S ribosomal subunits. Biochemistry. 14: 1060–1067.
Spencer, M., Pigram, W. J., and Littlechild, J. 1969. Studies on rRNA structure. Biochim. Biophys. Acta. 179: 348–359.
Spierer, P, Zimmermann, R. A., and Mackie, G. A. 1975. RNA-protein interactions in the ribosome. Eur. J. Biochem. 52: 459–468.
Spirin, A. S. 1969. Informosomes. Eur. J. Biochem. 10: 20–35.
Stadler, H. 1974. The primary structure of the 16 S rRNA binding protein S8 from E. coli. ribosomes. FEBS Lett. 48: 114–116.
Stadler, H., and Wittmann-Liebold, B. 1976. Determination of the amino-acid sequence of the ribosomal protein S8 of E. coli. Eur. J. Biochem. 66: 49–56.
Stavnezer, J., and Juang, R. C. C. 1971. Synthesis of a mouse immunoglobin light chain in a rabbit reticulocyte cell-free system. Nature New Biol. 230: 172–176.
Steitz, J. A. 1969. Polypeptide chain initiation. Nature. 224: 957–964.
Steitz, J. A. 1973. Discriminatory ribosome rebinding of isolated regions of protein synthesis initiation from the RNA of bacteriophage R17. Proc. Nat. Acad. Sci. USA. 70: 2605–2609.
Stevens, A. R., and Pachler, P. F. 1972. Discontinuity of 26 S rRNA inAcanthamoeba castellani. J. Mol. Biol. 66: 225–237.
Steward, D. L., Shaeffer, J. R., and Humphrey, R. M. 1968. Breakdown and assembly of polyribosomes in synchronized Chinese hamster cells. Science. 161: 791–793.
Stewart, J. W., Sherman, F., Shipman, N. A., and Jackson, M. 1971. Identification and mutational relocation of the AUG codon initiating translation of iso-l-cytochrome c. in yeast. J. Biol. Chem. 246: 7429–7445.
Stiles, C. D., Lee, K.-L., and Kenney, F. T. 1976. Differential degradation of mRNAs in mammalian cells. Proc. Nat. Acad. Sci. USA. 73: 2634–2638.
Stöffier, G., Hasenbank, R., Bodley, J. W., and Highland, J. H. 1974. Inhibition of protein L7/L12 binding to 50 S ribosomal cores by antibodies specific for L6, L10, and L18. J. Mol. Biol. 86: 171–174.
Stöffler, G., Wool, I. G., Lin, A., and Rak, K.-H. 1974. The identification of the eukaryotic ribosomal proteins homologous with E. coli. proteins L7 and L12. Proc. Nat. Acad. Sci. USA. 71: 4723–4726.
Stoltzfus, C. M., Shatkin, A. J., and Banerjee, A. K. 1973. Absence of poly(A) from reovirus mRNA. J. Biol. Chem. 248: 7993–7998.
Strycharz, W. A., Ranki, M., and Dahl, H. H. M. 1974. A high-molecular-weight protein component required for natural messenger translation in ascites tumor cells. Eur. J. Biochem. 48: 303–310.
Subramanian, A. R. 1974. Sensitive separation procedure for E. coli. ribosomal proteins and the resolution of high-molecular-weight components. Eur. J. Biochem. 45: 541–546.
Subramanian, A. R., and Davis, B. D. 1970. Activity of IF3 in dissociating E. coli. ribosomes. Nature. 228: 1273–1275.
Subramanian, A. R., Ron, E. Z., and Davis, B. D. 1968. A factor required for ribosome dissociation in E. coli. Proc. Nat. Acad. Sci. USA. 61: 761–767.
Sundaric, R. M., Stringer, E. A. Schulman, L. D. H., and Maitra, U. 1976. Interaction of bacterial IF-2 with initiator tRNA. J. Biol. Chem. 251: 3338–3345.
Sundquist, B., Persson, T., and Lindberg, U. 1977. Characterization of mRNA-protein complexes from mammalian cells. Nucl. Acids Res. 4: 899–915.
Sussman, M. 1966. Protein synthesis and the temporal control of genetic transcription during slime mold development. Proc. Nat. Acad. Sci. USA. 55: 813–818.
Szer, W., Hermoso, J. M., and Leffler, S. 1975. Ribosomal protein Si and polypeptide chain initiation in bacteria. Proc. Nat. Acad. Sci. USA. 72: 2325–2329.
Szer, W., and Leffler, S. 1974. Interaction of E. coli. 30 S ribosomal subunits with MS2 phage RNA in the absence of initiation factors. Proc. Nat. Acad. Sci. USA 71: 3611–3615.
Takagi, M., Tanaka, T., and Ogatu, K. 1970. Chromosome activity and cell function in polytenic cells. Biochim. Biophys. Acta 217: 108–119.
Tate, W. P., Beaudet, A. L., and Caskey, C. T. 1973. Influence of guanine nucleotides and elongation factors on interaction of release factors with the ribosome. Proc. Nat. Acad. Sci. USA. 70: 2350–2352.
Terao, K., and Ogata, K. 1975. Studies on structural proteins of the rat liver ribosomes. Biochim. Biophys. Acta. 402: 214–229.
Teraoka, H., and Tanaka, K. 1973. Effect of polyamines on the binding of dihydrostreptomycin and N-acetylphenylalanyl-tRNA to ribosomes from E. coli. Eur. J. Biochem. 40: 423429.
Terhorst, C., Möller, W., Laursen, R., and Wittmann-Liebold, B. 1973. The primary structure of an acidic protein which is involved in GTP hydrolysis dependent on elongation factors G and T. Eur. J. Biochem. 34: 138–152.
Terhorst, C., Wittmann-Liebold, B., and Möller, W. 1972. 50 S ribosomal proteins. Eur. J. Biochem. 25: 13–19.
Toivonen, J. E., and Nierlich, D. P. 1974. Biological decay of the 5’-triphosphate termini of the RNA of E. coli. Nature. 252: 74–76.
Träeger, L. 1970. Termination der Proteinsynthese. Naturwissenschaften. 57: 560–564.
Tsiapalis, C. M., Dorson, J. W., De Sante, D. M., and Bollum, F. J. 1973. Terminal riboadenylate transferase. Biochem. Biophys. Res. Comm. 50: 737–743.
Tsurugi, K., Morita, T., and Ogata, K. 1974. Mode of degradation of ribosomes in regenerating rat liver in vivo. Eur. J. Biochem. 45: 119–126.
Ulbrich, B., and Nierhaus. K. H., 1975. Pools of ribosomal proteins in E. coli. Eur. J. Biochem. 57: 49–54.
Van, N. T., Holder, J. W., Woo, S. L. C., Means, A. R., and O’Malley, B. W. 1976. Secondary structure of ovalbumin mRNA. Biochemistry. 15: 2054–2062.
Vandekerckhove, J., Francq, H., and Van Montagu, M. 1969. The amino acid sequence of the coat protein of the bacteriophage MS-2 and localization of the amber mutation in the coat mutants growing on a sul suppressor. Arch. Intern. Physiol. Biochim. 77: 175–180.
Vandekerckhove, J., Rombauts, W., Peeters, B., and Wittmann-Liebold, B. 1975. Determination of the complete amino-acid sequence of protein S21 from E. coli. Hoppe-Seyler’s Z. Phys. Chem. 356: 1955–1976.
Vandekerckhove, J., Rombauts, B., and Wittmann-Liebold, B. 1977. The primary structure of protein S16 from E. coli. ribosomes. FEBS Lett. 73: 18–21.
Van de Walle, C. 1973. Poly(A) sequences in plant RNA. FEBS Lett. 34: 31–34.
Van Dieijen, G., Van der Laken, C. J., van Knippenberg, P. H., and Van Duin, J. 1975. Function of E. coli. ribosomal protein S1 in translation of natural and synthetic mRNA. J. Mol. Biol. 93: 351–366.
Van Duin, J., and van Knippenberg, P. H. 1974. Requirement of protein S1 for translation. J. Mol. Biol. 84: 185–195.
Van Duin, J., van Knippenberg, P. H., Dieben, M., and Kurland, C. G. 1972. Functional heterogeneity of the 30 S ribosomal subunit of E. coli. Mol. Gen. Genetics. 116: 181–191.
van Knippenberg, P. H. 1975. A possible role of the 5’-terminal sequence of 16 S rRNA in the recognition of initiation sequences for protein synthesis. Nucl. Acids Res. 2: 79–85.
van Knippenberg, P. H., Hooykass, P. J. J., and Van Duin, J. 1974. The stoichiometry of E. coli 30S ribosomal protein S1 on in vivo and in vitro polyribosomes. FEBS Lett. 41: 323–326.
Vaquero, C., Reibel, L., Delaunay, J., and Schapiro, G. 1973. Translation of globin mRNA among eukaryotes. Biochem. Biophys. Res. Comm. 54: 1171–1177.
Vaughn, M. H., and Hansen, D. S., 1973. Control of initiation of protein synthesis in human cells. J. Biol. Chem. 248: 7087–7096.
Vigne, R., Jordan, B. R., and Monier, R. 1973. A common conformational feature in several prokaryotic and eukaryotic 5 S RNAs. J. Mol. Biol. 76: 303–311.
Visentin, L. P., Matheson, A. T., and Yaguchi, M. 1974. Homologies in procaryotic ribosomal proteins. FEBS Lett. 41: 310–314.
Volckaert, G., and Fiers, W. 1973. Studies on the bacteriophage MS2. G-U-G as the initiation codon of the A-protein cistron. FEBS Lett. 35: 91–96.
Volkin, E., and Astrachan, L. 1956. Phosphorus incorporation in E. coli. RNA after infection with bacteriophage T2. Virology. 2: 149–161.
Vournakis, J., and Rich, A. 1972. Ribosomal transformations during protein synthesis. In: Cox, R. A., and A. A. Hadjiolov, eds., Functional Units in Protein Biosynthesis., New York, Academic Press, p. 287–299.
Wade, M., Laursen, R. A., and Miller, D. L. 1975. Amino acid sequence of EF-Tu. FEBS Lett. 53: 37–39.
Wahba, A. J., Mazumder, R., Iwasaki, K., Choe, Y. B., Miller, M. J., Sillero, M. A. G., and Ochoa, S. 1968. Role of ribosome factors in polypeptide chain initiation. Abstr. Fed. Eur. Biochem. Soc., Madrid., p. 9.
Wahba, A. J., and Miller, M. J. 1974. Chain initiation factors from E. coli. Meth. Enzym. 30: 3–18.
Walker, T. A., Betz, J. L., Olah, J., and Pace, N. R. 1975. The nucleotide sequence of dolphin and bovine 5 S rRNA. FEBS Lett. 54: 241–244.
Weber, K., and Koenigsberg, W. 1967. Amino acid sequence of the f2 coat protein. J. Biol. Chem. 242: 3563–3578.
Wegnez, M., Monier, R., and Denis, H. 1972. Sequence heterogeneity of 5 S RNA in Xenopus laevis. FEBS Lett. 25: 13–20.
Wei, C. M., Gershowitz, A., and Moss, B. 1976. 5’-terminal and internal methylated nucleotide sequences in HeLa cell mRNA. Biochemistry. 15: 397–401.
Weiner, A. M., and Weber, K. 1973. A single UGA codon functions as a natural termination signal in the coliphage Qß coat protein cistron. J. Mol. Biol. 80: 837–855.
Weissbach, H., Redfield, B., and Moon, H. M. 1973. Further studies on the interactions of EF-1 from animal tissues. Arch. Biochem. Biophys. 156: 267–275.
Weissmann, C., Billeter, M. A., Goodman, H. M., Hindley, J., and Weber, H. 1973. Structure and function of phage RNA. Ann. Rev. Biochem. 42: 303–328.
Welfie, H., Stahl, J., and Bielka, H. 1972. Studies on proteins of animal ribosomes. FEBS Lett. 26: 228–232.
Wells, G. N., and Beevers, L. 1974. Protein synthesis in the cotyledons of Pisum sativum. L. Biochem. J. 139: 61–69.
Wen, W. N., León, P. E., and Hague, D. R. 1974. Multiple gene sites for 5 S and 18 + 28 S RNA on chromosomes of Glyptotendipes barvipes. J. Cell Biol. 62: 132–144.
Westover, K. C., and Jacobson, L. A. 1974. Control of protein synthesis in E. coli. J. Biol. Chem. 249: 6272–6279.
White, H. B., Laux, B. E., and Dennis, D. 1972. Messenger RNA structure: Compatibility of hairpin loops with protein sequence. Science. 175: 1264–1266.
Wice, M., and Kennell, D. 1974. Decay of mRNA from the tryptophan operon of E. coli. as a function of growth temperature. J. Mol. Biol. 84: 649–652.
Wigle, D. T., and Smith, A. E. 1973. Specificity in initiation of protein synthesis in a fractionated mammalian cell-free system. Nature New Biol. 242: 136–140.
Williamson, A. R., and Schweet, R. 1964. Role of the genetic message in initiation and release of the polypeptide chain. Nature. 202: 435–437.
Williamson, R. 1973. The protein moieties of animal messenger ribonucleoproteins. FEBS Lett. 37: 1–6.
Williamson, R., and Brownlee, G. G. 1969. The sequence of 5 S ribosomal RNA from two mouse cell lines. FEBS Lett. 3: 306–308.
Williamson, R., Morrison, M., Lanyon, G., Eason, R., and Paul, J. 1971. Properties of mouse globin mRNA and its preparation in milligram quantities. Biochemistry. 70: 3014–3020.
Wittmann, H. G. 1976. Structure, function and evolution of ribosomes. Eur. J. Biochem. 61: 1–13.
Wittmann-Liebold, B. 1973. Studies on the primary structure of 20 proteins from E. coli. ribosomes by means of an improved protein sequenator. FEBS Lett. 36: 247–249.
Wittmann-Liebold, B., and Dzionara, M. 1976a. Comparison of amino acid sequences among ribosomal proteins of E.coli. FEBS Lett. 61: 14–19.
Wittman-Liebold, B., and Dzionara, M. 1976b. Studies on the significance of sequence homologies among proteins from E. coli. ribosomes. FEBS Lett. 65: 281–283.
Wittmann-Liebold, B., Greuer, B., and Pannenbecker, R. 1975. The primary structure of protein L32 from the 50 S subunit of E. coli. ribosomes. Hoppe-Seyler’s Z. Phys. Chem. 356: 1977–1979.
Wittman-Liebold, B., Marzinzig, E., and Lehmann, A. 1976. Primary structure of protein S20 from the small ribosomal subunit of E. coli. FEBS Lett. 68: 110–114.
Wittmann-Liebold, B., and Pannenbecker, R. 1976. Primary structure of protein L33 from the large subunit of the E. coli. ribosome. FEBS Lett. 68: 115–118.
Woese, C. R. 1972. Evolution of macromolecular complexity. J. Theor. Biol. 33: 29–34.
Woledge, J., Corry, M. J., and Payne, P. I. 1974. Ribosomal RNA homologies in flowering plants. Biochim. Biophys. Acta. 349: 339–350.
Wong, J. T. F. 1975. A co-evolution theory of the genetic code. Proc. Nat. Acad. Sci. USA. 72: 1909–1912.
Wong, K. L., Bolton, P. H., and Kearns, D. R. 1975. Tertiary structure in E. coli. tRNAArg and tRNAva’ Biochim. Biophys. Acta. 383: 446–451.
Wong, Y. P., Reid, B. R., and Kearns, D. R. 1973. Conformation of charged and uncharged tRNAPhe. Proc. Nat. Acad. Sci. USA. 70: 2193–2195.
Woodley, C. L., Chen, Y. C., and Gupta, N. K. 1974. Purification and properties of the peptide chain initiation factors from rabbit reticulocytes. Methods Enzymol. 30: 141–153.
Yaguchi, M. 1975. Primary structure of protein S18 from the small E. coli. ribosomal subunit. FEBS Lett. 59: 217–220.
Yaguchi, M., Matheson, A. T., and Visentin, L. P. 1974. Procaryotic ribosomal proteins: N-terminal sequence homologies and structural correspondence of 30 S ribosomal proteins from E. coli. and Bacillus stearothermophilus. FEBS Lett. 46: 296–300.
Yamada, Y., Whitaker, P. A., and Nakada, D. 1974. Functional instability of T7 early mRNA. Nature. 248: 335–338.
Yanofsky, C., and Ito, J. 1966. Nonsense codons and polarity in the tryptophan operon. J. Mol. Biol. 21: 313–334.
Yams, M. 1972. Phenylalanyl-tRNA synthetase and isoteucy1-tRNAphe: A possible verification mechanism for aminoacyl-tRNA. Proc. Nat. Acad. Sci. USA. 69: 1915–1919.
Yarus, M., and Barrell, B. G. 1971. The sequence of nucleotides in tRNA1e from E. coli. B. Biochem. Biophys. Res. Comm. 43: 729–733.
Yogo, Y., and Wimmer, E. 1972. Poly(A) at the 3’-terminus of poliovirus RNA. Proc. Nat. Acad. Sci. USA. 69: 1877–1882.
Yokosawa, H., Inoue-Yokosawa, N., Arai, K.-i., Kawakita, M., and Kaziro, Y. 1973. The role of guanosine triphosphate hydrolysis in EF-Tu-promoted binding of aminoacyl tRNA to ribosomes. J. Biol. Chem. 248: 375–377.
Yu, R. S. T., and Wittmann, H. G. 1973. The sequence of steps in the attachment of 5 S RNA ta cores of E. coli. ribosomes. Biochim. Biophys. Acta. 324: 375–385.
Zalik, S., and Jones, B. L. 1973. Protein biosynthesis. Ann. Rev. Plant Physiol. 24: 47–68.
Zasloff, M., and Ochoa, S. 1971. A supernatant factor involved in initiation complex formation with eukaryotic ribosomes. Proc. Nat. Acad. Sci. USA. 68: 3059–3063.
Zasloff, M., and Ochoa, S. 1973. Polypeptide chain initiation in eukaryotes. J. Mol. Biol. 73: 65–76.
Zinder, N. 1963. Properties of a bacteriophage containing RNA. Perspectives Virol. 3: 58–67.
Zylber, E. A., and Penman, S. 1971. Synthesis of 5 S and 4 S RNA in metaphase-arrested HeLa cells. Science. 172: 947–949.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1978 Plenum Press, New York
About this chapter
Cite this chapter
Dillon, L.S. (1978). The Genetic Mechanism: II The Cell’s Employment of DNA. In: The Genetic Mechanism and the Origin of Life. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2436-2_4
Download citation
DOI: https://doi.org/10.1007/978-1-4684-2436-2_4
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-2438-6
Online ISBN: 978-1-4684-2436-2
eBook Packages: Springer Book Archive