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Reactive Sites and the Evolution of Transfer RNAs

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The Genetic Mechanism and the Origin of Life

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Abstract

Before the evolutionary relations of tRNAs can be examined, those specific sites in tRNA molecular structure that are of possible importance in a particular function need examination, in order to distinguish functional and evolutionary influences. Among the activities in which a given nucleotide may be especially significant are included the maintenance of a secondary or tertiary structure, recognition by the ligase, and attachment to the ribosome, as well as those codon—anticodon interactions that have already received attention (Chapter 7; Section 7.2).

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References

Chapters 7 and 8: Primary Structure of tRNAs

  • Barrell, B. G., Coulson, A. R., and McClain, W. H. 1973. Nucleotide sequence of a glycine tRNA coded by bacteriophage T4. FEBS Lett. 37: 64–69.

    Article  PubMed  CAS  Google Scholar 

  • Hill, C. W., Combriato, G., Stemhart, W., Riddle, D. L., and Carbon, J. 1973. The nucleotide sequence of the GGG-specific glycine tRNA of E. coli. and Salmonella typhimurium. J. Biol. Chem. 248: 4252–4262.

    CAS  Google Scholar 

  • Hill, C. W., Squires, C., and Carbon, J. 1970. Structural genes for two glycine tRNA species. J. Mol. Biol. 52: 557–569.

    Article  PubMed  CAS  Google Scholar 

  • Marcu, K., Mignery, R., Reszelbach, R., Roe, B., Sirover, M., and Dudock, B. 1973. The absense of ribothymidine in specific tRNAs. I. Glycine and threonine tRNAs of wheat embryo. Biochem. Biophys. Res. Comm. 55: 477–483.

    Article  PubMed  CAS  Google Scholar 

  • Riddle, D. L., and Carbon, J. 1973. Frameshift suppression: A nucleotide addition in the anticodon of a glycine tRNA. Nature New Biol. 242: 230–234.

    PubMed  CAS  Google Scholar 

  • Roberts, R. J. 1972: Structures of two glycyl-tRNAs from Staphylococcus epidermidis. Nature New Biol. 237: 44–46.

    Article  CAS  Google Scholar 

  • Roberts, R. J. 1974. Staphylococcal tRNAs. II. Sequence analysis of isoaccepting glycine tRNA IA and IB from Staphylococcus epidermidis. Texas 26. J. Biol. Chem. 249: 4787–4796.

    PubMed  CAS  Google Scholar 

  • Roberts, R. J., Lovinger, G. G., Tamura, T., and Strominger, J. L. 1974. Staphylococcal tRNAs. I. Isolation and purification of the isoaccepting glycine tRNAs from Staphylococcus epidermidis. Texas 26. J. Biol. Chem. 249: 4781–4786.

    PubMed  CAS  Google Scholar 

  • Squires, C., and Carbon, J. 1971. Normal and mutant glycine tRNAs. Nature New Biol. 233: 274–277.

    PubMed  CAS  Google Scholar 

  • Stahl, S., Paddock, G., and Abelson, J. 1973. T4 bacteriophage tRNA°1. Biochem. Biophys. Res. Comm. 54: 567–569.

    Article  PubMed  CAS  Google Scholar 

  • Stewart, T. S., Roberts, R. J., and Strominger, J. L. 1971. Novel species of RNA. Nature. 230: 36–38.

    Article  PubMed  CAS  Google Scholar 

  • Yoshida, M. 1973. The nucleotide sequence of tRNAch from yeast. Biochem. Biophys. Res. Comm. 50: 779–784.

    Article  PubMed  CAS  Google Scholar 

  • Zachau, H. G. 1969. Transfer ribonucleic acids. Angew. Chem. (Int. Ed.). 8: 711–727.

    Article  CAS  Google Scholar 

  • Holley, R. W., Apgar, J., Everett, G. A., Madison, J. T., Marquisee, M., Merrill, S. H., Penswrick, J. R., and Zamir, A. 1965a. Structure of a ribonucleic acid. Science., 147: 1462–1465.

    Article  PubMed  CAS  Google Scholar 

  • Holley, R. W., Everett, G. A., Madison, J. T., and Zamir, A. 1965b. Nucleotide sequences in the yeast alanine tRNA. J. Biol. Chem. 240: 2122–2127.

    PubMed  CAS  Google Scholar 

  • Merrill, C. R. 1968. Reinvestigation of the primary structure of yeast alanine tRNA. Biopolymers. 6: 1727–1735.

    Article  Google Scholar 

  • Murao, K., Hasegawa, T., and Ishikura, H. 1976. 5-methoxyuridine: A new minor constituent located in the first position of the anticodon of tRNAma, tRNAThr, and tRNAval from B. subtilis. Nucl. Acids Res. 3:2851–2857.

    Google Scholar 

  • Penswick, J. R., Martin, R., and Dirheimer, G. 1975. Evidence supporting a revised sequence for yeast alanine tRNA. FEBS Lett. 50: 28–31.

    Article  PubMed  CAS  Google Scholar 

  • Takemura, S., and Ogawa, K. 1973. The primary structure of alanine tRNAI from Torulopsis utilis. J. Biochem. 74: 323–333.

    CAS  Google Scholar 

  • Takemura, S., Ogawa, K., and Nakazawa, K. 1972. Nucleotide sequence of alanine tRNA, from Torulopsis utilis. FEBS Lett. 25: 29–32.

    Article  CAS  Google Scholar 

  • Takemura, S., Ogawa, K., and Nakazawa, K. 1973. The primary structure of alanine tRNAI from Torulopsis utilis. J. Biochem. 74: 313–322.

    CAS  Google Scholar 

  • Williams, R. J., Nagel, W., Roe, B., and Dudock, B. 1974. Primary structure of E. coli. alanine tRNA: Relation to the yeast phenylalanyl tRNA synthetase recognition site. Biochem. Biophys. Res. Comm. 60: 1215–1221.

    Article  PubMed  CAS  Google Scholar 

  • Yoshida, M., Kaziro, Y., and Ukita, T. 1968. Evidence for the important role of inosine residue in codon recognition of yeast alanine tRNA. Biochim. Biophys. Acta. 166: 646–655.

    PubMed  CAS  Google Scholar 

  • Gangloff, J., Keith, G., Ebel, J. P., and Dirheimer, G. 1971. Structure of asparate-tRNA from brewer’s yeast. Nature New Biol. 230: 125–126.

    Article  PubMed  CAS  Google Scholar 

  • Gangloff, J., Keith, G., Ebel, J. P., and Dirheimer, G. 1972a. The primary structure of aspartate tRNA from brewer’s yeast. Complete digestion with pancreatic ribonuclease and T, ribonuclease. Biochim. Biophys. Acta. 259: 198–209.

    PubMed  CAS  Google Scholar 

  • Gangloff, J., Keith, G., Ebel, J. P., and Dirheimer, G. 1972b. The primary structure of aspartate

    Google Scholar 

  • tRNA from brewer’s yeast. II. Partial digestions with pancreatic ribonuclease and T1 ribonuclease and derivation of complete sequence. Biochim. Biophys. Acta. 259: 210–222.

    Google Scholar 

  • Harada, F., and Nishimura, S. 1972. Possible anticodon sequences of tRNA’, tRNAAS“, and tRNAAaP from E. coli. B. Universal presence of nucleoside Q in the first position of the anticodon of these transfer ribonucleic acids. Biochemistry. 11: 301–308.

    Article  PubMed  CAS  Google Scholar 

  • Harada, F., Yamaizumi, K., and Nishimura, S. 1972. Oligonucleotide sequences of RNase T1 and pancreatic RNase digests of E. coli. aspartic acid tRNA. Biochem. Biophys. Res. Comm. 49: 1605–1609.

    Article  PubMed  CAS  Google Scholar 

  • Keith, G., Gangloff, J., Ebel, J. P., and Dirheimer, G. 1970. Etablissement de la sĂ©quence de nuclĂ©otides de l’aspartate-t-RNA de levure de bière. C. R. Acad. Sci. Paris., 271: 613–616.

    CAS  Google Scholar 

  • Kobayashi, T., Irie, T., Yoshida, M., Takeishi, K., and Ukita, T. 1974. The primary structure of yeast glutamic acid tRNA specific to the GAA codon. Biochim. Biophys. Acta. 366: 168–181.

    PubMed  CAS  Google Scholar 

  • Munninger, K. O., and Chang, S. H. 1972. A fluorescent nucleoside from glutamic acid tRNA of E. coli. K12. Biochem. Biophys. Res. Comm. 46: 1837–1842.

    Article  PubMed  CAS  Google Scholar 

  • Ohashi, Z., Murao, K., Yahagi, T., von Minden, D. L., McCloskey, J. A., and Nishimura, S. 1972. Characterization of C+ located in the first position of the anticodon of E. coli. tRNAMet as N4-acetylcytidine. Biochim. Biophys. Acta. 262: 209–213.

    CAS  Google Scholar 

  • Ohashi, Z., Saneyoshi, M., Harada, F., Hara, H., and Nishimura, S. 1970. Presumed anticodon structure of glutamic acid tRNA from E. coli: A possible location of a 2-thiouridine derivative in the first position of the anticodon. Biochem. Biophys. Res. Comm. 40: 866–872.

    Article  CAS  Google Scholar 

  • Singhal, R. P. 1971. Modification of E. coli. glutamate tRNA with bisulfite. J. Biol. Chem. 246: 5848–5851.

    PubMed  CAS  Google Scholar 

  • Yoshida, M., Takeishi K., and Ukita, T. 1970. Anticodon structure of GAA-specific glutamic acid tRNA from yeast. Biochem. Biophys. Res. Comm. 39: 852–857.

    Article  PubMed  CAS  Google Scholar 

  • Yoshida, M., Takeishi, K., and Ukita, T. 1971. Structural studies on a yeast glutamic acid tRNA specific to GAA codon. Biochim. Biophys. Acta. 228: 153–166.

    PubMed  CAS  Google Scholar 

  • Bayev, A. A., Venkstern, T. V., Mirzabekov, A. D., Krutilina, A. I., Li, L., and Axelrod, V. D. 1967. Primary structure of the valine tRNA. Mol. Biol. 1: 754–758.

    Google Scholar 

  • Bonnet, J., Ebel, J. P., and Dirheimer, G. 1971. Primary structure of tRNA)a’, from brewer’s yeast. FEBS Lett. 15: 286–290.

    Article  PubMed  CAS  Google Scholar 

  • Bonnet, J., Ebel, J. P., Dirheimer, G., Shershneva, L. P., Krutilina, A. I., Venkstern, T. V., and Bayer, A. A. 1974. The corrected nucleotide sequence of valine tRNA from baker’s yeast. Biochimie. 56: 1211–1213.

    Article  PubMed  CAS  Google Scholar 

  • Harada, F., Kimura, F., and Nishimura, S. 1969. Nucleotide sequence of valine tRNA from E. coli. B. Biochim. Biophys. Acta. 195: 590–592.

    PubMed  CAS  Google Scholar 

  • Harada, F., Kimura, F., and Nishimura, S. 1971. Primary sequence of tRNA’, from E. coli. B. Biochemistry. 10: 3269–3283.

    Article  PubMed  CAS  Google Scholar 

  • Kimura-Harada, F., Saneyoshi, M., and Nishimura, S. 1971. 5-methyl-2-thiouridine: A new sulfur-containing minor constituent from rat liver glutamic acid and lysine tRNAs. FEBS Lett. 13: 335–338.

    Google Scholar 

  • Mirzavekov, A. D., Lastit, D., Leoina, E. S., Undritsov, I. M., and Baev, A. A. 1972. The acceptor activity of dissected baker’s yeast tRNA°a1: Localization of two possible recognition sites of valyl-tRNA ligase. Mol. Biol. 6: 69–84.

    PubMed  CAS  Google Scholar 

  • Mizutani, T., Miyazaki, M., and Takemura, S. 1968. The primary structure of valine-I tRNA from Torulopsis utilis. J. Biochem. 64: 839–848.

    CAS  Google Scholar 

  • Murao, K., Saneyoshi, M., Harada, F., and Nishimura, S. 1970. Uridin-5-oxyacetic acid: A new minor constituent from E. coli. tRNA I. Biochem. Biophys. Res. Comm. 38: 657–662.

    Article  PubMed  CAS  Google Scholar 

  • Piper, P. W. 1975b. The primary structure of the major cytoplasmic valine tRNA of mouse myeloma cells. Eur. J. Biochem. 51: 295–304.

    Article  PubMed  CAS  Google Scholar 

  • Piper, P. W., and Clark, B. F. 1974a. The nucleotide sequences of cytoplasmic methionine and valine tRNAs from mouse myeloma cells. FEBS Lett. 47: 56–59.

    Article  PubMed  CAS  Google Scholar 

  • Takada-Gurrier, C., Grosjean, H. G., Dirheimer, G., and Keith, G. 1976. The primary structure of tRNA2a’ from B. stearothermophilus. FEBS Lett. 62: 1–3.

    Article  Google Scholar 

  • Takemura, S., Mizutani, T., and Miyazaki, M. 1968a. The primary structure of valine-I tRNA from Torulopsis utilis. J. Biochem. 63: 277–278.

    CAS  Google Scholar 

  • Takemura, S., Mizutani, T., and Miyazaki, M. 1968b. The primary structure of valine-I tRNA from Torulopsis utilis. I. Complete digestion with pancreatic ribonuclease and ribonuclease T1. J. Biochem. 64: 827–837.

    PubMed  CAS  Google Scholar 

  • Yaniv, M., and Barrell, B. G. 1969. Nucleotide sequence of E. coli. B tRNAva’. Nature. 222: 278–279.

    Article  PubMed  CAS  Google Scholar 

  • Yaniv, M., and Barrell, B. G. 1971. Sequence relationship of three valine acceptor tRNAs from E. coli. Nature New Biol. 233: 113–114.

    CAS  Google Scholar 

  • Zachau, H. G. 1972. Transfer ribonucleic acids. In: Bosch, L., ed., The Mechanism of Protein Synthesis and its Regulation., Amsterdam, North-Holland Publishing Co., p. 173–217.

    Google Scholar 

  • Blank, H. U., and Sö11, D. 1971. The nucleotide sequence of two leucine tRNA species from E. coli. K12. Biochem. Biophys. Res. Comm. 43: 1192–1197.

    Article  PubMed  CAS  Google Scholar 

  • Dube, S. K., Marcker, K. A., and Yudelevich, A. 1970. The nucleotide sequence of a leucine tRNA from E. coli. FEBS Lett. 9: 168–170.

    Article  CAS  Google Scholar 

  • Harada, F., Sato, S., and Nishimura, S. 1972. Unusual CCA-stem structure of E. coli. B tRNA1 s FEBS Lett. 19: 352–355.

    CAS  Google Scholar 

  • Singer, C. E., and Smith, G. R. 1972. Histidine regulation in Salmonella typhimurium. XIII. Nucleotide sequence of histidine tRNA. J. Biol. Chem. 247: 2983–3000.

    Google Scholar 

  • Singer, C. E., Smith, G. R., Cortese, R., and Ames, B. N. 1972. Mutant tRNA’ ineffective in repression and lacking two pseudouridine modifications. Nature New Biol. 238: 73–74.

    Article  Google Scholar 

  • Comer, M. M., Foss, K., and McClain, W. H. 1975. A mutation of the wobble nucleotide of a bacteriophage T4 tRNA. J. Mol. Biol. 99: 283–293.

    Article  PubMed  CAS  Google Scholar 

  • Folk, W. R., and Yaniv, M. 1972. Coding properties and nucleotide sequences of E. coli. glutamine tRNAs. Nature New Biol. 237: 165–166.

    PubMed  CAS  Google Scholar 

  • Seidman, J. G., Corner, M. M., and McClain, W. H. 1974. Nucleotide alterations in the bacteriophage T4 glutamine tRNA that affect ochre suppressor activity. J. Mol. Biol. 90: 677–689.

    Article  PubMed  CAS  Google Scholar 

  • Murao, K., Tanabe, T., Ishii, F., Namiki, M., and Nishimura, S. 1972. Primary sequence of arginine tRNA from E. coli. Biochem. Biophys. Res. Comm., 47: 1332–1337.

    Article  CAS  Google Scholar 

  • Weissenbach, J., Martin, R., and Dirheimer, G. 1972. Nucleotide sequence of tRNAiltrg from brewer’s yeast. FEBS Lett. 28: 353–355.

    Article  PubMed  CAS  Google Scholar 

  • Weissenbach, J., Martin, R., and Dirheimer, C. 1975a. The primary structure of tRNAr from brewer’s yeast. Eur. J. Biochem. 56: 521–526.

    Article  PubMed  CAS  Google Scholar 

  • Weissenbach, J., Martin, R., and Dirheimer, G., 1975. Partial digestion with Ti RNase and primary sequence of yeast tRNAllrg. Eur. J. Biochem. 56: 527–532.

    Article  PubMed  CAS  Google Scholar 

  • Barrell, B. G., Seidman, J. G., Guthrie, C., and McClain, W. H. 1974.. Transfer RNA biosynthesis: The nucleotide sequence of a precursor to serine and proline tRNAs. Proc. Nat. Acad. Sci. USA. 71: 413–416.

    Google Scholar 

  • Seidman, J. G., Barrell, B. G., and McClain, W. H. 1975. Five steps in the conversion of a large precusor RNA into bacteriophage proline and serine tRNAs. J. Mol. Biol. 99: 733–760.

    Article  PubMed  CAS  Google Scholar 

  • Madison, J. T., and Boguslawski, S. J. 1974. Partial digestion of a yeast lysine tRNA and reconstruction of the nucleotide sequence. Biochemistry. 13: 524–527.

    Article  PubMed  CAS  Google Scholar 

  • Madison, J. T., Boguslawski, S. J., and Teetor, G. H. 1972. Nucleotide sequence of a lysine tRNA from baker’s yeast. Science. 176: 687–689.

    Article  PubMed  CAS  Google Scholar 

  • Madison, J. T., Boguslawski, S. J., and Teetor, G. H. 1974. Oligonucleotide composition of a yeast lysine tRNA. Biochemistry. 13: 518–523.

    Article  PubMed  CAS  Google Scholar 

  • Smith, C. J., Ley, A. N., D’Obrenan, P., and Mitra, S. K. 1971. The structure and coding specificity of a lysine tRNA from the haploid yeast S. cerevisiae. aS288C. J. Biol. Chem., 246: 7817–7829.

    PubMed  CAS  Google Scholar 

  • Smith, C. J., Teh, H. S., Ley, A. N., and D’Obrenan, P. 1973. The nucleotide sequences of the major and minor lysine tRNAs from the haploid yeast S. cerevisiae. aS288C. J. Biol. Chem. 248: 4475–4485.

    PubMed  CAS  Google Scholar 

  • Harada, F., and Nishimura, S. 1974. Purification and characterization of AUA specific isoleucine tRNA from E. coli. B. Biochemistry. 13: 300–307.

    Article  PubMed  CAS  Google Scholar 

  • Takemura, S., Murakami, M., and Miyazaki, M. 1969a. Nucleotide sequence of isoleucine tRNA from Torulopsis utilis. J. Biochem. 65: 489–491.

    CAS  Google Scholar 

  • Takemura, S., Murakami, M., and Miyazaki, M., 1969b. The primary structure of isoleucine tRNA from Torulopsis utilis. J. Biochem. 65: 553–566.

    CAS  Google Scholar 

  • Yarus, M., and Barre11, B. G. 1971. The sequence of nucleotides in tRNAne from E. coli. B. Biochem. Biophys. Res. Comm. 43: 729–733.

    Article  PubMed  CAS  Google Scholar 

  • Cory, S., and Marcker, K. A. 1970. The nucleotide sequence of methionine tRNAM. J. Biochem. 12: 177–194.

    CAS  Google Scholar 

  • Cory, S., Marcker, K. A., Dube, S. K., and Clark, B. F. C. 1968. Primary structure of a methionine tRNA from E. coli. Nature. 220: 1039–1040.

    CAS  Google Scholar 

  • Dube, S. K., and Marcker, K. A. 1969. The nucleotide sequence of N-formyl-methionyl-transfer RNA. Eur. J. Biochem. 8: 256–262.

    Article  PubMed  CAS  Google Scholar 

  • Dube, S. K., Marcker, K. A., Clark, B. F. C., and Cory, S. 1968. Nucleotide sequence of Nformyl-methionyl-transfer RNA. Nature. 218: 233–234.

    Article  Google Scholar 

  • Dube, S. K. Marcker, K. A., Clark, B. F. C., and Cory, S. 1969. The nucleotide sequence of Nformyl-methionyl-transfer RNA. Eur. J. Biochem. 8: 244–255.

    CAS  Google Scholar 

  • Ecarot-Charrier, B., and Cedergren, R. J. 1976. The preliminary sequence of tRNAFet from Anacystis nidulans. compared with other initiator tRNAs. FEBS Lett. 63: 287–290.

    Article  PubMed  CAS  Google Scholar 

  • Egan, B. Z., Weiss, J. F., and Kelmers, A. D. 1973. Separation and comparison of primary structures of three formylmethionine tRNAs from E.coli. K-12MO. Biochem. Biophys. Res. Comm. 55: 320–327.

    Article  PubMed  CAS  Google Scholar 

  • Gruhl, H., and Feldmann, H. 1975. The primary structure of a noninitiating methionine specific tRNA from brewer’s yeast. FEBS Lett. 57: 145–148.

    Article  PubMed  CAS  Google Scholar 

  • Högenauer, G., Turnowsky, F., and Unger, F. M. 1972. Codon-anticodon interaction of methionine specific tRNAs. Biochem. Biophys. Res. Comm. 46: 2100–2106.

    Article  PubMed  Google Scholar 

  • Ishikura, H., Yamada, Y., Murao, K., Saneyoshi, M., and Nishimura, S. 1969. The presence of N- [9-(β-D-ribofuranosyl)purine-6yl-carbomoyl]threonine in serine, methionine, and lysine tRNAs from E. coli. Biochem. Biophys. Res. Comm. 37: 990–995.

    Article  CAS  Google Scholar 

  • Koiwai, O., and Miyazaki, M. 1976. The primary structure of non-initiator tRNAMgit from baker’s yeast. J. Biochem. 80: 951–959.

    PubMed  CAS  Google Scholar 

  • Petrissant, G., and Boisnard, M. 1974. ParticularitĂ©s structurales du mĂ©thionine tRNA,M„et de foie de lapin. Biochimie. 56: 787–789.

    Article  PubMed  CAS  Google Scholar 

  • Piper, P. W. 1975a. The nucleotide sequence of a methionine tRNA which functions in protein elongation in mouse myeloma cells. Eur. J. Biochem. 51: 283–293.

    Article  PubMed  CAS  Google Scholar 

  • Piper, P. W., and Clark, B. F. C. 1974b. Primary structure of a mouse myeloma cell initiator tRNA. Nature. 247: 516–518.

    Article  PubMed  CAS  Google Scholar 

  • Simsek, M., and RajBhandary, U. L. 1972. The primary structure of yeast initiator tRNA. Biochem. Biophys. Res. Comm. 49: 508–515.

    Article  PubMed  CAS  Google Scholar 

  • Simsek, M., RajBhandary, U. L., Boisnard, M. and Petrissant G. 1974. Nucleotide sequence of rabbit liver and sheep mammary gland cytoplasmic initiator tRNAs. Nature. 247: 518–520.

    Article  PubMed  CAS  Google Scholar 

  • Yamada, Y., and Ishikura, H. 1975. Nucleotide sequence of initiator tRNA from B. subtilis. FEBS Lett. 54: 155–158.

    Article  CAS  Google Scholar 

  • Ish-Horowicz, D., and Clark, B. F. C. 1973. The nucleotide sequence of a serine tRNA from E. coli. J. Biol. Chem. 248: 6663–6673.

    CAS  Google Scholar 

  • Rogg, H., MĂĽller, P., and Staehelin, M. 1975. Nucleotide sequences of rat liver serine tRNA. Eur. J. Biochem. 53: 115–127.

    Article  CAS  Google Scholar 

  • Yamada, Y., and Ishikura, H. 1973. Nucleotide sequence of tRNA3er from E. coli. FEBS Lett. 29: 231–234.

    Article  CAS  Google Scholar 

  • Clarke, L., and Carbon, J. 1974. The nucleotide sequence of a threonine tRNA from E. coli. J. Biol. Chem. 249: 6874–6885.

    CAS  Google Scholar 

  • Kuntzel, B., Weissenbach, J. and Dirheimer, G. 1972. The sequence of nucleotides in tRNAftig from brewer’s yeast. FEBS Lett. 25: 189–191.

    Article  PubMed  CAS  Google Scholar 

  • Kuntzel, B., Weissenbach, J., and Dirheimer, G. 1974. Structure primaire des tRNAfirg de levure de bière. Biochimie. 56: 1069–1087.

    Article  PubMed  CAS  Google Scholar 

  • Blobstein, S. H., Grunberger D., Weinstein, I. B., and Nakanishi, K. 1973. Isolation and structure determination of the fluorescent base from bovine liver phenylalanine tRNA. Biochemistry. 12: 188–193.

    Article  PubMed  CAS  Google Scholar 

  • Dudock, B. S., and G. Katz. 1969. Large oligonucleotide sequences in wheat germ phenylalanine tRNA. J. Biol. Chem., 244: 3069–3074.

    PubMed  CAS  Google Scholar 

  • Dudock, B. S., Katz, G., Taylor, E. K., and Holley, R. W. 1969. Primary structure of wheat germ phenylalanine tRNA. Proc. Nat. Acad. Sci. USA. 62: 941–945.

    Article  PubMed  CAS  Google Scholar 

  • Everett, G. A., and Madison, J. T. 1976. Nucleotide sequence of tRNAPhe from pea (Pisum sativum., Alaska). Biochemistry. 15: 1016–1021.

    Article  PubMed  CAS  Google Scholar 

  • Guerrier-Takada, C., Dirheimer, G., Grosjean, H., and Keith, G. 1975. The primary structure of tRNAPhe from Bacillus stearothermophilus. FEBS Lett. 60: 286–289.

    Article  CAS  Google Scholar 

  • Harbers, K., Thiebe, R., and Zachau, H. G. 1972. Preparation and characterization of fragments from yeast tRNAPhe. Eur. J. Biochem. 26: 132–143.

    Article  PubMed  CAS  Google Scholar 

  • Keith, G., Ebel, J. P., and Dirheimer, G. 1974. The primary structure of two mammalian tRNAsPhe: Identity of calf liver and rabbit liver tRNAsPhe. FEBS Lett. 48: 50–52.

    Article  PubMed  CAS  Google Scholar 

  • Keith, G., Picaud, F., Weissenbach, J., Ebel, J. P., Petrissant, G., and Dirheimer, G. 1973. The primary structure of rabbit liver tRNAPhe and its comparison with known tRNAPhe sequences. FEBS Lett. 31: 345–347.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H., Quigley, G. J., Suddath, F. L., McPherson, A., Sneden, D., Kim, J. J., Weinzierl, J., and Rich, A. 1973. Three-dimensional structure of yeast phenylalanine tRNA: Folding of the polynucleotide chain. Science. 179: 285–288.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H.,. Suddath, F. L., Quigley, G. J., McPherson, A., Sussman, J. L., Wang, A. H. J., Seeman, N. C., and Rich, A. 1974. Three-dimensional tertiary structure of yeast phenylalanine tRNA. Science. 185: 435–440.

    CAS  Google Scholar 

  • Nakanishi, K., Furutachi, N., Funamizu, M., Grunberger, D., and Weinstein, I. B. 1970. Structure of the fluorescent Y base from yeast phenylalanine tRNA. J. Am. Chem. Soc. 92: 7617–7619.

    Article  PubMed  CAS  Google Scholar 

  • Philippsen, P., and Zachau, H. G. 1971. Fragments of yeast tRNAPhe and tRNASer prepared by partial digestion with spleen phosphodiesterase. FEBS Lett. 15: 69–74.

    Article  PubMed  CAS  Google Scholar 

  • Pongo, O., Bald, R., and Reinwald, E. 1973. On the structure of yeast tRNAPhe: Complementaryoligonucleotide binding studies. Eur. J. Biochem. 32: 117–125.

    Article  Google Scholar 

  • RajBhandary, U. L., Chang, S. H., Sneider, J., and Davis, D. 1968. Yeast phenylalanine tRNA: Partial digestion with ribonuclease T1, and derivation of the total primary structure. J. Biol. Chem. 243: 598–608.

    Google Scholar 

  • RajBhandary, U. L., Chang, S. H., Stuart, A., Faulkner, R. D., Hoskinson, R. M., and Khorana, H. G. 1967. The primary structure of yeast phenylalanine tRNA. Proc. Nat. Acad. Sci. USA. 57: 751–758.

    Article  Google Scholar 

  • Rosenfeld, A., Stevens, C. L., and Printz, M. P. 1970. Studies on the secondary structure of phenylalanyl tRNA. Biochemistry. 9: 4971–4980.

    Article  PubMed  CAS  Google Scholar 

  • Takemura, S., Kasai, H., and Goto, M. 1974. Nucleotide sequence of the anticodon region of Torulopsis. phenylalanine tRNA. J. Biochem. 75: 1169–1172.

    PubMed  CAS  Google Scholar 

  • Uziel, M., and Gassen, H. G. 1969. Structure of tRNAPke. Fed. Proc. 28: 409.

    Google Scholar 

  • Wong, Y. P., Kearns, D. R., Shulman, R. G., Yamane, T., Chang, S., Chirskyian, J. G., and Fresco, J. R. 1973. High resolution NMR study of base pairing in the native and denatured conformers of tRNA. J. Mol. Biol. 74: 403–406.

    Article  PubMed  CAS  Google Scholar 

  • Altman, S., and Smith, J. D. 1971. Tyrosine tRNA precursor molecule polynucleotide sequence. Nature New Biol. 233: 35–39.

    PubMed  CAS  Google Scholar 

  • Doctor, B. P., Loebel, J. E., and Kellog, D. A. 1966. Studies on the species specificity of yeast and E. coli. tyrosine tRNA2. Cold Spring Harbor Symp. Quant. Biol. 31: 543–548.

    Article  PubMed  CAS  Google Scholar 

  • Doctor, B. P., Loebel, J. E., Sodd, M. A. and Winter, D. B. 1969. Nucleotide sequence of E. coli. tyrosine tRNA. Science. 163: 693–695.

    Article  PubMed  CAS  Google Scholar 

  • Goodman, H. M., Abelson, J. N., Landy, A., Brenner, S., and Smith, J. D. 1968. Amber suppression: A nucleotide change in the anticodon of a tyrosine tRNA. Nature. 217: 1019–1024.

    Article  PubMed  CAS  Google Scholar 

  • Goodman, H. M., Abelson, J. N., Landy, A., Zadrazil, S., and Smith, J. D. 1970. The nucleotide sequences of tyrosine tRNAs of E. coli. Eur. J. Biochem. 13: 461–483.

    CAS  Google Scholar 

  • Harada, F., Gross, H. J., Kimura, F., Chang, S. H., Nishimura, S., and RajBhandary, U. L. 1968. 2-methylthio N6-(12-isopentenyl) adenosine: A component of E. coli. tyrosine tRNA. Biochem. Biophys. Res. Comm. 33: 299–306.

    Google Scholar 

  • Hashimoto, S., Miyazaki, M., and Takemura, S. 1969. Nucleotide sequence of tyrosine tRNA from Torulopsis utilis. J. Biochem. 65: 659–661.

    CAS  Google Scholar 

  • Hachimoto, S., Takemura, S., and Miyazaki, M. 1972. Partial digestion with ribonuclease T, and derivation of the complete sequence of tRNATYr from Torulopsis utilis. J. Biochem. 72: 123–134.

    Google Scholar 

  • Madison, J. T., Everett, G. A., and Kung, H. 1966a. Nucleotide sequence of a yeast tyrosine tRNA. Science. 153: 531–534.

    Article  PubMed  CAS  Google Scholar 

  • Madison, J. T. Everett, G. A., Kung, H. 1966b. On the nucleotide sequence of yeast tyrosine tRNA. Cold Spring Harbor Symp. Quant. Biol. 31: 409–416.

    Article  CAS  Google Scholar 

  • Madison, J. T., Everett, G. A., Kung, H. 1967. Oligonucleotides from yeast tyrosine tRNA. J. Biol. Chem. 242: 1318–1323.

    PubMed  CAS  Google Scholar 

  • Madison, J. T., and Kung, 11.-K. 1967. Large oligonucleotides isolated from yeast tyrosine tRNA after partial digestion with ribonuclease T1. Science. 242: 1324–1330.

    CAS  Google Scholar 

  • Seno, T., and Nishimura, S. 1971. Cleavage of E. coli. tyrosine tRNA2 in S-region and its effects on the structure and function of the reconstituted molecules. Biochim. Biophys. Acta. 228: 141–152.

    PubMed  CAS  Google Scholar 

  • Takemura, S., Hashimoto, S., and Miyazaki, M. 1972. Complete digestion of tyrosine tRNA from Torulopsis utilis. with pancreatic and T1 ribonucleases. J. Biochem. 72: 111–121.

    PubMed  CAS  Google Scholar 

  • Ginsberg, T., Rogg, H., and Staehelin, M. 1971. Nucleotide sequences of rat liver serine-tRNA. Eur. J. Biochem. 21: 249–257.

    Article  PubMed  CAS  Google Scholar 

  • Hentzen, D., and Garet, J. P. 1976. Anticodon loop sequences of tRNAccA and tRNA cA from the posterior silkgland of Bombyx mori. L. Biochem. Biophys. Res. Comm. 71: 241–248.

    Article  PubMed  CAS  Google Scholar 

  • Ishikura, H., Yamada, Y., and Nishimura, S. 1971a. The nucleotide sequence of a serine tRNA from E. coli. FEBS Lett. 16: 68–70.

    Article  CAS  Google Scholar 

  • Ishikura, H., Yamada, Y., and Nishimura, S. 1971b. Structure of serine tRNA from E. coli. Biochim. Biophys. Acta. 228: 471–481.

    CAS  Google Scholar 

  • McClain, W. H., Barrell, B. G., and Seidman, J. G. 1975. Nucleotide alterations in bacteriophage T4 serine tRNA that affect the conversion of precursor RNA into tRNA. J. Mol. Biol. 99: 717–732.

    Article  PubMed  CAS  Google Scholar 

  • Rogg, H., and Staehelin, M. 1971a. Nucleotide sequences of rat liver serine-tRNA. 1. Products of digestion with pancreatic ribonuclease. Eur. J. Biochem. 21: 235–242.

    Article  PubMed  CAS  Google Scholar 

  • Rogg, H., and Staehelin, M. 1971b. Nucleotide sequence of rat liver serine-tRNA. 2. The products of digestion with ribonuclease T1. Eur. J. Biochem. 21: 243–248.

    Article  PubMed  CAS  Google Scholar 

  • Staehelin, M. 1971. The primary structure of tRNA. Experientia., 27: 1–11.

    Article  PubMed  CAS  Google Scholar 

  • Staehelin, M., Rogg, H., Baguley, B. C., Ginsberg, T., and Wehrli, W. 1968. Structure of a mammalian serine tRNA. Nature. 219: 1363–1365.

    Article  PubMed  CAS  Google Scholar 

  • Zachau, H. G., DĂĽtting, D., and Feldmann, H. 1966a. Nucleotidsequenzen zweier serinspezifischer Transfer-Ribonucleinsäuren. Angew. Chem., 78: 392–393.

    Article  Google Scholar 

  • Zachau, H. G., DĂĽtting, D., and Feldmann, H. 1966b. Serine specific tRNAs. Hoppe-Seyler’s Z. Phys. Chem. 347: 229–235.

    Google Scholar 

  • Hirsch, D. 1970. Tryptophan tRNA of E. coli. Nature. 228: 57.

    Google Scholar 

  • Hirsch, D. 1971. Tryptophan tRNA as the UGA suppressor. J. Mol. Biol. 58: 439–458.

    Article  Google Scholar 

  • Keith, G., Roy, A., Ebel, J. P., and Dirheimer, G. 1971. The nucleotide sequences of two tryptophan-tRNAs from brewer’s yeast. FEBS Lett. 17: 306–308.

    Article  PubMed  CAS  Google Scholar 

  • Maugh, T. H. 1974. Rous sarcoma virus: A new role for tRNA. Science. 186: 41.

    Article  PubMed  Google Scholar 

  • Chang, S. H., Kuo, S., Hawkins, E., and Miller, N. R., 1973. The corrected nucleotide sequence of yeast leucine tRNA. Biochem. Biophys. Res. Comm. 51: 951–955.

    Article  PubMed  CAS  Google Scholar 

  • Chang, S. H., and Miller, N. 1971. The nucleotide sequence of yeast leucine tRNA. Fed. Proc. 30: 1101.

    Google Scholar 

  • Kowalski, S., Yamane, T., and Fresco, J. R. 1971. Nucleotide sequence of the “denaturable” leucine tRNA from yeast. Science. 172: 385–387.

    Article  PubMed  CAS  Google Scholar 

  • Pinkerton, T. C., Paddock, G., and Abelson, J. 1972. Bacteriophage T4 tRNA Leu. Nature New Biol. 240: 88–90.

    Article  PubMed  CAS  Google Scholar 

  • Pinkerton, T. C., Paddock, G., and Abelson, J. 1973. Nucleotide sequence determination of bacteriophage T4 leucine tRNA. J. Biol. Chem. 248: 6348–6365.

    PubMed  CAS  Google Scholar 

  • Holness, N.J., and Atfield, G. 1974. Nucleotide sequence of tRNAcys from baker’s yeast. FEBS Lett. 46: 268–270.

    Article  PubMed  CAS  Google Scholar 

  • Holness, N. J., and Atfield, G. 1976a. The extraction and purification of a cysteine tRNA from baker’s yeast. Biochem. J. 153: 429–435.

    PubMed  CAS  Google Scholar 

  • Holness, N. J., and Atfield, G. 1976b. The nucleotide sequence of cysteine tRNA from baker’s yeast. Biochem. J. 153: 447–454.

    PubMed  CAS  Google Scholar 

  • Abraham, D. J. 1971. Proposed detailed structural model for tRNA and its geometric relationship to a messenger. J. Theor. Biol. 30: 83–91.

    Article  PubMed  CAS  Google Scholar 

  • Allende, J. E., and Allende, C. C. 1971. Detection ?nd isolation of complexes between aminoacyltRNA synthetases and their substrates. Meth. Enzym. 20: 210–220.

    Article  Google Scholar 

  • Bhargava, P. M. 1971. Aminoacyl-tRNA synthetase recognition code-words in yeast tRNAs-a proposal. J. Theor. Biol. 29: 447–469.

    Article  Google Scholar 

  • Bina-Stein, M., and Crothers, D. M. 1974. Conformational changes of tRNA. Biochemistry. 13: 2771–2775.

    Article  PubMed  CAS  Google Scholar 

  • Blanquet, S., Fayat, G., Poiret, M., and Waller, J. P. 1975. The mechanism of action of methionyl-RNA synthetase from E. coli. Eur. J. Biochem. 51: 567–571.

    CAS  Google Scholar 

  • Bolton, P. H., and Kearns, D. R. 1975. NMR evidence for common tertiary structure base pairs in yeast and E. coli. tRNA. Nature. 255: 347–349.

    Article  PubMed  CAS  Google Scholar 

  • Briand, J. P., Jonard, G., Guilley, H., Richards, K., and Hirth, L. 1977. Nucleotide sequence (n = 159) of the amino-acid-accepting 3’-OH extremity of TYMV RNA. Eur. J. Biochem., 72: 453–463.

    Article  PubMed  CAS  Google Scholar 

  • Briand, J. P., Richards, K. E., Bouley, J. P., Witz, J., and Hirth, L. 1976. Structure of the amino-acid accepting 3’-end of high-molecular-weight eggplant mosaic virus RNA. Proc. Nat. Acad. Sci. USA. 73: 737–741.

    Article  PubMed  CAS  Google Scholar 

  • Budzik, G. P., Lam, S. S. M., Schoemaker, H. J. P., and Schimmel, P. R. 1975. Two photo cross-linked complexes of isoleucine specific tRNA with aminoacyl tRNA synthetases. J. Biol. Chem. 250: 4433–4439.

    PubMed  CAS  Google Scholar 

  • Carbon, J., and Curry, J. B. 1968. Genetically and chemically derived missense suppressor tRNAs with altered enzymatic aminoacylation rates. J. Mol. Biol. 38: 201–216.

    Article  PubMed  CAS  Google Scholar 

  • Carbon, J., and Fleck, E. W. 1974. Genetic alteration of structure and function in glycine tRNA of E. coli: Mechanism of suppression of the tryptophan synthetase A78 mutation. J. Mol. Biol. 85: 371–391.

    Article  PubMed  CAS  Google Scholar 

  • Caron, M., Brisson, N., and Dugas. H. 1976. Evidence for a conformational change in tRNAPhe upon aminoacylation. J. Biol. Chem. 251: 1529–1530.

    PubMed  CAS  Google Scholar 

  • Cedergren, R. J., Cordeau, J. R., and Robillard, P. 1972. On the phylogeny of tRNAs. J. Theor. Biol. 37: 209–220.

    Article  PubMed  CAS  Google Scholar 

  • Celis, J. E., Hooper, M. L., and Smith, J. D. 1973. Amino acid acceptor stem of E. coli. suppressor tRNATYr is a site of synthetase recognition. Nature New Biol. 244: 261–264.

    PubMed  CAS  Google Scholar 

  • Chambers, R. W. 1971. On the recognition of tRNA by its aminoacyl-tRNA ligase. Progr. Nucl. Acid Res. Mol. Biol. 11: 489–525.

    Article  CAS  Google Scholar 

  • Chambers, R. W., Aoyagi, S., Furukawa, Y., Zawadzka, H., and Bhanot, O. S. 1973. Inactivation of valine acceptor activity by a CU missense change in the anticodon of yeast valine tRNA. J. Biol. Chem. 248: 5549–5551.

    PubMed  CAS  Google Scholar 

  • Chapeville, F., Lipmann, F., von Ehrenstein, G., Weisblum, B., Ray, W. J., and Benzes, S. 1962. On the role of soluble RNA in coding for amino acids. Proc. Nat. Acad. Sci. USA. 48: 1086–1092.

    Article  PubMed  CAS  Google Scholar 

  • Chapeville, F., and Rouget, P. 1972. Aminoacyl-tRNA synthetases. Frontiers Biol. 27: 5–32.

    CAS  Google Scholar 

  • Chatterjee, S. K. and Kaji, H. 1970. Conformational changes of tRNA on aminoacylation. Biochim. Biophys. Acta. 224: 88–98.

    PubMed  CAS  Google Scholar 

  • Chinali, G., Sprinzl, M., Parmeggioni, A., and Cramer, F. 1974. Participation in protein biosynthesis of tRNA bearing altered 3’-terminal ribosyl residues. Biochemistry. 13: 3001–3010.

    Article  PubMed  CAS  Google Scholar 

  • Cole, P. E., and Crothers, D. M. 1972. Conformational changes of tRNA. Biochemistry. 11: 4368–4374.

    Article  PubMed  CAS  Google Scholar 

  • Cole, P. E., Yang, S. K., and Crothers, D. M. 1972. Conformational changes of tRNA. Equilibrium phase diagrams. Biochemistry. 11: 4358–4368.

    Article  PubMed  CAS  Google Scholar 

  • Cramer, F. 1971. Three-dimensional structure of tRNA. Progr. Nucl. Acid Res. Mol. Biol. 11: 391–421.

    Article  CAS  Google Scholar 

  • Dayhoff, M. O., and McLaughlin, P. J. 1972. Early evolution: Transfer RNA. In: Dayhoff, M. O., ed., Atlas of Protein Sequence and Structure. Vol. 5. National Biomedical Research Foundation, Washington, D.C., p. 111–118.

    Google Scholar 

  • Delaney, P., Bierbaum, J., and Ofengand, J. 1974. Conformational changes in thiouridine region of E. coli. tRNA as assessed by photochemically induced cross-linking. Arch. Biochem. Biophys. 161: 260–267.

    Article  CAS  Google Scholar 

  • Dube, S. K. 1973. Evidence for “three-point” attachment of tRNA to methionyl tRNA synthetase. Nature New Biol. 243: 103–105.

    Article  PubMed  CAS  Google Scholar 

  • Eisinger, J., and Gross, N. 1975. Conformers, dimers, and anticodon complexes of tRNAr (E. coli). Biochemistry. 14: 4031–4040.

    Article  CAS  Google Scholar 

  • Elder, K. T., and Smith, A. E. 1973. Methionine tRNA of avian myeloblastosis virus. Proc. Nat. Acad. Sci. USA. 70: 2823–2826.

    Article  PubMed  CAS  Google Scholar 

  • Evans, J. A., and Nazario, M. 1974. Neurospora. arginyl tRNA ligase binding and dissoaciation of tRNA. Biochemistry. 13: 3092–3098.

    CAS  Google Scholar 

  • Fasiolo, F., Befort, N., Boulanger, Y., and Ebel, J. P. 1970. Purification et quelques propriĂ©tĂ©s de la phĂ©nylalanyl-tRNA synthĂ©tase de levure de boulangerie. Biochim. Biophys. Acta. 217: 305–318.

    PubMed  CAS  Google Scholar 

  • Fasiolo, F., and Ebel, J. P. 1974. Yeast phenylalanyl tRNA synthetase. Eur. J. Biochem. 49: 257–263.

    Article  PubMed  CAS  Google Scholar 

  • Fasiolo, F., Renny, P., Pouyet, J., and Ebel, J. P. 1974. Yeast phenylanlanyl-tRNA synthetase. Eur. J. Biochem. 50: 227–236.

    Article  PubMed  CAS  Google Scholar 

  • Gamble, R. C., and Schimmel, P. R. 1974. Transfer RNA conformation in solution investigated by isotope labeling. Proc. Nat. Acad. Sci. USA. 71: 1356–1360.

    Article  PubMed  CAS  Google Scholar 

  • Gangloff, J., Dirheimer, G., and Gangloff, M. L. 1973. Studies on aspartyl-tRNA synthetase from baker’s yeast. Biochim. Biophys. Acta. 294: 263–272.

    CAS  Google Scholar 

  • Glick, J. M., and Leboy, P. S. 1977. Purification and properties of tRNA (adenine-1)-methyltransferase from rat liver. J. Biol. Chem. 252: 4790–4795.

    PubMed  CAS  Google Scholar 

  • Gros, C., Lemaire, G., Rapenbusch, R. V., and Labouesse, B. 1972. The subunit structure of tryptophanyl tRNA synthetase from beef pancreas. J. Biol. Chem. 247: 2931–2943.

    PubMed  CAS  Google Scholar 

  • Gross, H. J. 1973. Transfer RNA: Evidence for decreasing size variation during evolution. J. Mol. Evol. 2: 339–342.

    Article  PubMed  CAS  Google Scholar 

  • Guilley, H., Jonard, G., and Hirth, L. 1975. Sequence of 71 nucleotides at the 3’-end of tobacco. mosaic virus RNA. Proc. Nat. Acad. Sci. USA. 72: 864–868.

    Article  PubMed  CAS  Google Scholar 

  • Haines, J. A., and Zamecnik, P. C. 1967. Chemical modification of aminoacyl ligases and the effect on formation of aminoacyl-tRNAs. Biochim. Biophys. Acta. 146: 227–238.

    PubMed  CAS  Google Scholar 

  • Hanke, T., Bartmann, P., Hennecke, H., Kosakowski, H. M., Jaenicke, R., Holler, E., and Boeck, A. 1974. L-phenylalanyl-tRNA synthetase of E. coli. K-10; A reinvestigation of molecular weight and subunit structure. Eur. J. Biochem. 43: 601–607.

    Article  PubMed  CAS  Google Scholar 

  • Harpold, M. A., and Calvin, M. 1973. A simple model of the amino acid acceptor terminus of a tRNA. Biochim. Biophys. Acta. 308: 117–128.

    PubMed  CAS  Google Scholar 

  • Hashimoto, S., Kawata, M., and Takemura, S. 1972a. Reconstitution of an active acceptor com- plex which lacks the anticodon of Torulopsis. tyrosine tRNA. J. Biochem. 72: 1339–1349.

    PubMed  CAS  Google Scholar 

  • Hashimoto, S., Takemura, S., and Miyazaki, M. 1972b. Partial digestion with ribonuclease Ti and derivation of the complete sequence of tyrosine tRNA from Torulopsis utilis. J. Biochem. 72: 123–134.

    CAS  Google Scholar 

  • Hashimoto, S., Takemura, S., Yabuki, S., Konishi, K., and Samejima, T. 1972c. Physicochemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis. tyrosine tRNA. J. Biochem. 72: 1185–1195.

    PubMed  CAS  Google Scholar 

  • Hecht, S. M., Kozarich, J. W., and Schmidt, F. J. 1974. Isomeric phenylalanyl-tRNAs. Position of the aminoacyl moiety during protein biosynthesis. Proc. Nat. Acad. Sci. USA. 71: 4317–4321.

    Article  PubMed  CAS  Google Scholar 

  • Heider, H., Gottschalk, E., and Cramer, F. 1971. Isolation and characterization of seryl-tRNA synthetase from yeast. Eur. J. Biochem. 20: 144–152.

    Article  PubMed  CAS  Google Scholar 

  • Hennecke, H., and Böck, A. 1975. Altered a subunits in phenylalanyl-tRNA synthetases from p.fluorophenylalanine-resistant strains of E. coli. Eur. J. Biochem. 55: 431–437.

    CAS  Google Scholar 

  • Hirshfield, I. N., and Bloemers, H. P. J. 1969. The biochemical characterization of two mutant arginyl tRNA synthetases from E. coli. K-12. J. Biol. Chem. 244: 2911–2916.

    PubMed  CAS  Google Scholar 

  • Holler, E., Hammer-Rober, B., Hanke, T., and Bartmann, P. 1975. The catalytic mechanism of amino acid: tRNA ligases. Biochemistry. 14: 2496–2503.

    Article  PubMed  CAS  Google Scholar 

  • Holmquist, R., and Jukes, T. H. 1973. No evidence for a common evolutionary origin of 5 S rRNA and tRNA. Nature New Biol. 245: 127.

    Article  PubMed  CAS  Google Scholar 

  • Isham, K. R., and Stulberg, M. P. 1974. Modified nucleosides in under-methylated phenylalanine tRNA from E. coli. Biochim. Biophys. Acta. 340: 177–182.

    CAS  Google Scholar 

  • Jones, C. R., and Kearns, D. R. 1974. Investigations of the structure of yeast tRNAPhe by nuclear magnetic resonance: Paramagnetic rare earth ion probes of structure. Proc. Nat. Acad. Sci. USA. 71: 4237–4240.

    Article  PubMed  CAS  Google Scholar 

  • Jukes, T. H., and Holmquist, R. 1972. Evolution of tRNA molecules as a repetitive process. Biochem. Biophys. Res. Comm. 49: 212–216.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H. 1975. Symmetry recogniton hypothesis model for tRNA binding to aminoacyl tRNA synthetase. Nature. 256: 679–681.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H., Quigley, G. J., Suddath, F. L., McPherson, A., Sneden, D., Kim, J. J., Weinzierl, J., and Rich, A. 1973. Three dimensional structure of yeast phenylalanine tRNA; folding of the polynucleotide chain. Science. 179: 285–288.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H., Suddath, F. L., Quigley, G. J., McPherson, A., Sussman, J. L., Wang, A. H. J., Seeman, N. C., and Rich, A. 1974a. Three dimensional tertiary structure of yeast phenylalanine tRNA. Science. 185: 435–440.

    Article  PubMed  CAS  Google Scholar 

  • Kim, S. H., Sussman, J. L., Suddath, F. L., Quigley, G. J., McPherson, A., Wang, A. H., Seeman, N. C., and Rich, A. 1974b. The general structure of tRNA molecules. Proc. Nat. Acad. Sci. USA. 71: 4970–4974.

    Article  PubMed  CAS  Google Scholar 

  • Kiselev, L. L., and Favorova, O. O. 1974. Aminoacyl-tRNA synthetases: Some recent results and achievements. Adv. Enzymol. 40: 141–238.

    CAS  Google Scholar 

  • Koch, G. L. E., Boulanger, Y., and Hartley, B. S. 1974. Repeating sequences in aminoacyl-tRNA synthetases. Nature. 249: 316–320.

    Article  PubMed  CAS  Google Scholar 

  • Lamy, D., Jonard, G., Guilley, H., and Hirth, L. 1975. Comparison between the 3’OH end RNA

    Google Scholar 

  • sequence of two strains of TMV which may be aminoacylated. FEBS Lett. 60:202–204.

    Google Scholar 

  • Lapointe, J., and Söll, D. 1972a. Glutamyl tRNA synthetase of E. coli. I. Purification and properties. J. Biol. Chem. 247: 4966–4974.

    PubMed  CAS  Google Scholar 

  • Lapointe, J., and Söll, D. 1972b. Glutamyl tRNA synthetase of E. coli. II. Interaction with intact glutamyl tRNA. J. Biol. Chem. 247: 4975–4981.

    PubMed  CAS  Google Scholar 

  • Lawrence, F. 1973. Effect of adenosine on methionyl-tRNA synthetase. Eur. J. Biochem. 40: 493–500.

    Article  PubMed  CAS  Google Scholar 

  • Lawrence, F., Blanquet, S., Poiret, M., Robert-Gero, M., and Waller, J. P. 1973. Ion requirements and kinetic parameter of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes. Eur. J. Biochem. 36: 234–243.

    Article  PubMed  CAS  Google Scholar 

  • Lawrence, F., Shire, D. J., and Waller, J. P., 1974. The effect of adenosine analogues on the ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase. Eur. J. Biochem. 41: 73–81.

    Article  PubMed  CAS  Google Scholar 

  • Lemaire, G., Gros, C., Epely, S., Kaminski, M., and Labouesse, B. 1975. Multiple forms of tryptophanyl-tRNA synthetase from beef pancreas. Eur. J. Biochem. 51: 237–252.

    Article  PubMed  CAS  Google Scholar 

  • Lengyel, P., and Söll, D. 1969. Mechanism of protein biosynthesis. Bacteriol. Rev. 33: 264–301.

    PubMed  CAS  Google Scholar 

  • Levitt, M. 1969. Detailed molecular model for tRNA. Nature. 224: 759–763.

    Article  PubMed  CAS  Google Scholar 

  • Maelicke, A., Sprinzl, M., van der Haar, F., Khwaja, T. A., and Cramer, F. 1974. Structural studies on phenylalanine tRNA from yeast with the spectroscopic label formycin. Eur. J. Biochem. 43: 617–625.

    Article  PubMed  CAS  Google Scholar 

  • Marcu, K., Mignery, R., Reszelbach, R., Roe, B., Sirover, M., and Dudock, B. 1973. The absence of ribothymidine in specific eukaryotic tRNAs I. Glycine and threonine tRNAs of wheat embryo. Biochem. Biophys. Res. Comm. 55: 477–483.

    Article  PubMed  CAS  Google Scholar 

  • Marcu, K., et al. 1974. Personal communication.

    Google Scholar 

  • Mehler, A. H., and Mitra, S. K. 1967. The activation of arginyl tRNA synthetase by tRNA. J. Biol. Chem. 242: 5495–5499.

    PubMed  CAS  Google Scholar 

  • Muench, K. H., Lipscomb, M. S., Lee, M., and Kuehl, G. V. 1975. Homologous cysteine-containing sequences in tryptophanyl-tRNA synthetases from E. coli. and human placentas. Science. 187: 1089–1091.

    Article  PubMed  CAS  Google Scholar 

  • Mullins, D. W., Lacey, J. C., and Hearn, R. A. 1973a. 5 S rRNA and tRNA-evidence for a common evolutionary origin. Nature New Biol. 242: 80–81.

    Google Scholar 

  • Mullins, D. W., Lacey, J. C., and Hearn, R. A. 1973b. Reply. Nature New Biol. 245: 127–128.

    Article  Google Scholar 

  • Murayama, A., Raffin, J. P., Remy, P., and Ebel, J. P. 1975a. Yeast phenylalanyl-tRNA synthetase: Properties of the sulfhydryl groups; evidence for -SH requirements in tRNA acylation. FEBS Lett. 53: 15–22.

    Article  PubMed  CAS  Google Scholar 

  • Murayama, A., Raffin, J. P., Remy, P., and Ebel, J. P. 1975b. Yeast phenylalanyl-tRNA synthetase; isolation of subunits on organomercurial-sepharose columns. FEBS Lett. 53: 23–25.

    Article  PubMed  CAS  Google Scholar 

  • Nazario, M., and Evans, J. A. 1974. Physical and kinetic studies of arginyl tRNA ligase of Neurospora. J. Biol. Chem. 249: 4934–4942.

    CAS  Google Scholar 

  • Novelli, G. D. 1967. Amino acid activation for protein synthesis. Ann. Rev. Biochem. 36: 449–484.

    Article  PubMed  CAS  Google Scholar 

  • C.Aberg, B., and Philipson, L. 1972. Binding of histidine to TMV RNA. Biochem. Biophys. Res. Comm. 48: 927–932.

    Article  Google Scholar 

  • Odom, O. W., Hardesty, B., Wintermeyer, W., and Zachau, H. G. 1974. The effect of removal or replacement with proflavine of the Y base in the anticodon loop of yeast tRNAphe on binding into the acceptor or donor sites of reticulocyte ribosomes. Arch. Biochem. Biophys. 162: 536–551.

    Article  PubMed  CAS  Google Scholar 

  • Ofengand, J., Chlâdek, S., Robilard, G., and Bierbaum, J. 1974. Enzymatic acylation of oxydized reduced tRNA by E. coli., yeast, and rat liver synthetases occurs almost exclusively at the 2’ hydroxyl. Biochemistry. 13: 5425–5432.

    Article  PubMed  CAS  Google Scholar 

  • Ofengand, J., and Henes, C. 1969. The function of pseudouridylic acid in tRNA. J. Biol. Chem. 244: 6241–6253.

    PubMed  CAS  Google Scholar 

  • Papas, T. S., and Peterkofsky, A. 1972. A random sequential mechanism for arginyl tRNA synthetase of E. coli. Biochemistry. 11: 4602–4608.

    CAS  Google Scholar 

  • Parfait, R., and Grosjean, H. 1972. Arginyl-tRNA synthetase from Bacillus stearothermophilus. Eur. J. Biochem. 30: 242–249.

    Article  CAS  Google Scholar 

  • Penneys, N. S., and Muench, K. H. 1974. Human placental tryptophanyl tRNA synthetase. Biochemistry. 3: 560–565.

    Article  Google Scholar 

  • Petrissant, G. 1973. Evidence for the absence of the G-T-1,1,-C sequence from two mammalian initiator tRNAs. Proc. Nat. Acad. Sci. USA. 70: 1046–1049.

    Article  PubMed  CAS  Google Scholar 

  • Ravel, J. M., Wang, S. F., Heinemeyer, C., and Shive, W. 1965. Glutamyl and glutaminyl RNA synthetases of E. coli. J. Biol. Chem. 240: 432–438.

    CAS  Google Scholar 

  • Reid, B. R., Einarson, B., and Schmidt, J. 1972. Loop accessibility in tRNA. Biochimie. 54: 325–332.

    Article  CAS  Google Scholar 

  • Riesner, D., Maass, G., Thiebe, R., Philippsen, P., and Zachau, H. G. 1973. The conformational transitions in yeast tRNAPhe as studied with tRNAPhe fragments. Eur. J. Biochem. 36: 76–88.

    Article  PubMed  CAS  Google Scholar 

  • Roberts, J. W., and Carbon, J. 1974. Molecular mechanism for missense suppression in E. coli. Nature. 250: 412–414.

    CAS  Google Scholar 

  • Roberts, R. J., Lovinger, G. G., Tamura, T., and Strominger, J. L. 1974. Staphylococcal tRNAs. I. Isolation and purification of the isoaccepting tRNA from Staphylococcus epidermidis. Texas 26. J. Biol. Chem. 249: 4781–4786.

    PubMed  CAS  Google Scholar 

  • Roe, B., Michael, M., and Dudock, B. 1973. Function of NZ-methylguanine in phenylalanine tRNA. Nature New Biol. 246: 135–138.

    PubMed  CAS  Google Scholar 

  • Rymo, L., Lundvik, L., and Lagerkvist, U. 1972. Subunit structure and binding properties of three amino acid tRNA ligases. J. Biol. Chem. 247: 3888–3899.

    PubMed  CAS  Google Scholar 

  • Santi, D. V., Danenberg, P. V., and Satterly, P. 1971. Phenylalanyl tRNA synthetase from E.

    Google Scholar 

  • coli. Reaction parameters and order of substrate addition. Biochemistry. 10:4804–4812.

    Google Scholar 

  • Schmidt, J., Wang, R., Stanfield, S., and Reid, B. R. 1971. Yeast phenylalanyl tRNA synthetase. Biochemistry. 10: 3264–3268.

    Article  PubMed  CAS  Google Scholar 

  • Schoemaker, H. J. P., Budzik, G. P., GiegĂ©, R., and Schimmel, P. R. 1975. Three photocrosslinked complexes of yeast phenylalanine specific tRNA with aminoacyl tRNA synthetases. J. Biol. Chem. 250: 4440–4444.

    PubMed  CAS  Google Scholar 

  • Schoemaker, H. J. P., and Schimmel, P. R. 1974. Photo-induced joining of a tRNA with its cognate amino-acid-tRNA synthetase. J. Mol. Biol. 84: 503–513.

    Article  PubMed  CAS  Google Scholar 

  • Seno, T., Agris, P. F., and Söll, D. 1974. Involvement of the anticodon region of E. coli. tRNA°n and tRNA°u in the specific interaction with cognate aminoacyl-tRNA synthetase. Biochim. Biophys. Acta. 349: 328–338.

    PubMed  CAS  Google Scholar 

  • Shulman, R. G., Hilbers, C. W., Kearns, D. R., Reid, B. R., and Wong, Y. P. 1973. Ring-current shifts in the 300 MHz NMR spectra of six purified tRNA molecules. J. Mol. Biol. 78: 57–69.

    Article  PubMed  CAS  Google Scholar 

  • Simsek, M., Petrissant, G., and RajBhandary, U. L. I973a. Replacement of the sequence G-T-grC-G(A)- by G-A-U-C-G in initiator tRNA of rabbit liver cytoplasm. Proc. Nat. Acad. Sci. USA. 70: 2600–2604.

    Google Scholar 

  • Simsek, M., Ziegenmeyer, J., Heckman, J., and RajBhandary, U. L. 1973b. Absence of the sequence G-T-q,-C-G(A)- in several eukaryotic cytoplasmic initiator rRNAs. Proc. Nat. Acad. Sci. USA. 70: 1041–1045.

    Article  PubMed  CAS  Google Scholar 

  • Singer, C. E., Smith, G. R., Cortese, R., and Ames, B. N. 1972. Mutant tRNA’ ineffective in repression and lacking two pseudouridine modifications. Nature New Biol. 238: 72–74.

    PubMed  CAS  Google Scholar 

  • Singhal, R. P. 1971. Modification of E. coli. glutamate tRNA with bisulfite. J. Biol. Chem. 246: 5848–5851.

    PubMed  CAS  Google Scholar 

  • Singhal, R. P. 1974. Chemical probe of structure and function of tRNAs. Biochemistry. 13: 2924–2932.

    Article  PubMed  CAS  Google Scholar 

  • Sprinzl, M., and Cramer, F. 1973. Accepting site for aminoacylation of tRNAPhe from yeast. Nature New Biol. 245: 3–5.

    PubMed  CAS  Google Scholar 

  • Squires, C., and Carbon, J. 1971. Normal and mutant glycine tRNAs. Nature New Biol. 233: 274–277.

    PubMed  CAS  Google Scholar 

  • Steinberg, W. 1974. Temperature-induced depression of tryptophan biosynthesis in a tryptophanyltRNA synthetase mutant of B. subtilis. J. Bact. 117: 1023–1034.

    CAS  Google Scholar 

  • Suddath, F. L., Quigley, G. J., McPherson, A., Sneden, D., Kim, J. J., Kim, S. H., and Rich, A. 1974. Three dimensional structure of yeast phenylalanine tRNA at 3.0 resolution. Nature. 248: 20–24.

    Article  PubMed  CAS  Google Scholar 

  • Taglang, R., Waller, J. P., Befort, N., and Fasiolo, F. 1970. Amino-acylation du tRNAva’ de E. coli. par la phĂ©nylalanyl-tRNA synthĂ©tase de levure. Eur. J. Biochem. 12: 550–557.

    Article  PubMed  CAS  Google Scholar 

  • Tal, J., Deutscher, M. P., and Littauer, U. Z. 1972. Biological activity of E. coli. tRNAPhe modified in its C-C-A terminus. Eur. J. Biochem. 28: 478–491.

    Article  PubMed  CAS  Google Scholar 

  • Thiebe, R. 1975. Aminoacylation of tRNA. Magnesium requirement and spermidine effect. FEBS Lett. 51: 259–261.

    Article  PubMed  CAS  Google Scholar 

  • Thiebe, R., and Zachau, H. G. 1968. A special modification next to the anticodon of phenylalanine tRNA. Eur. J. Biochem. 5: 546–555.

    Article  PubMed  CAS  Google Scholar 

  • Thomas, G. J., Chen, M. C., and Hartman, K. A. 1973. Raman studies of nucleic acids. X. Conformational structure of E. coli. tRNAs in aqueous solution. Biochim. Biophys. Acta. 324: 37–49.

    PubMed  CAS  Google Scholar 

  • von Ehrenstein, G., Weisblum, B., and Benzer, S. 1963. The function of sRNA as amino acid adaptor in the synthesis of hemoglobin. Proc. Nat. Acad. Sci. USA. 49: 669–675.

    Article  PubMed  CAS  Google Scholar 

  • White, B. N., and Tener, G. M. 1973. Properties of tRNAPhe from Drosophila. Biochim. Biophys. Acta. 312: 267–275.

    CAS  Google Scholar 

  • Williams, R. J., Nagel, W., Roe, B., and Dudock, B. 1974. Primary structure of E. coli. alanine tRNA: Relation to the yeast phenylalanyl tRNA synthetase recognition site. Biochem. Biophys: Res. Comm. 60: 1215–1221.

    Article  CAS  Google Scholar 

  • Wolfenden, R., Rammler, D. H., and Lipmann, F. 1964. On the site of esterification of amino acids to soluble RNA. Biochemistry. 3: 329–338.

    Article  PubMed  CAS  Google Scholar 

  • Wong, Y. P., Reid, B. R., and Kearns, D. R. 1973. Conformation of charged and uncharged tRNAs. Proc. Nat. Acad. Sci. USA. 70: 2193–2195.

    Article  PubMed  CAS  Google Scholar 

  • Yang, C. H., and Söll, D. 1974. Studies of tRNA tertiary structure by singlet-singlet energy transfer. Proc. Nat. Acad. Sci. USA. 71: 2838–2842.

    Article  PubMed  CAS  Google Scholar 

  • Yang, S. K., and Crothers, D. M. 1972. Conformational changes of tRNA. Comparison of the early melting transition of two tyrosine-specific tRNAs. Biochemistry. 11: 4375–4381.

    Article  PubMed  CAS  Google Scholar 

  • Yem, D. W., and Williams, L. S. 1973. Evidence for the existence of two arginyl-tRNA synthetase activities in E. coli. J. Bact. 113: 891–894.

    CAS  Google Scholar 

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  1. Texas A & M University, College Station, Texas, USA

    Lawrence S. Dillon

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Dillon, L.S. (1978). Reactive Sites and the Evolution of Transfer RNAs. In: The Genetic Mechanism and the Origin of Life. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2436-2_8

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  • DOI: https://doi.org/10.1007/978-1-4684-2436-2_8

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