Abstract
Investigations on the structure of initiation complexes of protein biosynthesis are essential prerequisites for understanding the arrangement of the various components and their interactions at the molecular level. Initiation of protein biosynthesis in eukaryotic cells needs at least nine initiation factors (eIF-1, eIF-2, eIF-2B, eIF-3, eIF-4A, eIF-4B, eIF-4C, eIF-4F, and eIF-5) as described by Trachsel et al. (1977), Thomas etal. (1981), and Clemens etal. (1982) (for reviews see Jagus etal., 1981; Maitra etal., 1982). For analysis of the function of the individual initiation factors, different complexes were isolated and characterized. First the ternary complex of eIF-2-GTP-Met-tRNAf becomes bound to a 43S preinitiation complex that contains the small ribosomal subunit, eIF-3, and other factors (Sundkvist and Staehelin, 1975). Thereupon, mRNA is attached, forming a 48S preinitiation complex. After detachment of initiation factors from the 48S complex, the large ribosomal subunit associates, forming an 80S initiation complex.
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References
Baralle, F.E., Brownlee, G.G. (1978). AUG is the only recognisable signal sequence in the 5′ non-coding regions of eukaryotic mRNA. Nature 274: 84–87.
Bielka, H., Westermann, P., Nygärd, O., Stahl, J., Bommer, U.-A., Noll, F., Lutsch, G., Gross, B. (1982). Function and topography of components of initiation complexes of eukaryotic translation. In: Interaction of translational and transcriptional controls in the regulation of gene expression, eds. Grunberg-Manago, M., Safer, B. Elsevier Sei, Publ. Co., pp. 281–290.
Bolton, A.E., Hunter, W.M. (1973). The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay. Biochem. J. 133: 529–538.
Clemens, M.J., Pain, V.M., Wong, S.T., Henshaw, E.C. (1982). Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2. Nature 296: 93–95.
Emanuilov, I., Sabatini, D.D., Lake, J.A., Freienstein, C. (1978). Localization of eukaryotic initiation factor 3 on native small ribosomal subunits. Proc. Natl. Acad. Sei. USA 75: 1389–1393.
Erni, B., Staehelin, T. (1982). Base pair formation between 18S ribosomal RNA and globin mRNA during initiation of protein synthesis in vitro. FEBS Lett. 148: 79–82.
Evstafieva, A.G., Shatsky, I.N., Bogdanov, A.A., Semenkov, Y.P., Vasiliev, V.D. (1983). Localization of 5′ and 3′ ends of the ribosome-bound segment of template polynucleotides by immune electron microscopy. EMBO J. 2: 799–804.
Gross, B., Westermann, P., Bielka, H. (1983). Spatial arrangement of proteins within the small subunit of rat liver ribosomes studied by cross-linking. EMBO J. 2: 255–260.
Hansen, J., Etchison, D., Hershey, J.W.B., Ehrenfeld, E. (1982). Association of cap binding protein with eukaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected Hela cells. J. Virol. 42: 200–207.
Jagus, R., Anderson, W.F., Safer, B. (1981). The regulation of initiation of mammalian protein synthesis. Progr. Nucl. Acid Res. Mol. Biol. 25: 127–185.
Kaempfer, R., Kaufman, J. (1972). Translational control of hemoglobin synthesis by an initiation factor required for recycling of ribosomes and for their binding to messenger RNA. Proc. Natl. Acad. Sci. USA 69: 3317–3321.
Kozak, M. (1977). Nucleotide sequences of 5′-terminal ribosome-protected initiation regions from two reovirus messages. Nature 269: 390–394.
Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
Legon, S. (1976). Characterization of the ribosome-protected regions of 125I-labelled rabbit globin mRNA. J. Mol. Biol. 106: 37–53.
Lutsch, G., Benndorf, R., Westermann, P., Behlke, J., Bommer, U.-A., Bielka, H. (1985). On the structure of native small ribosomal subunits and initiation factor eIF-3 isolated from rat liver. Biomed. Biochim. Acta 44: K1 - K7.
Lutsch, G., Bielka, H., Enzmann, G., Noll, F. (1983). Electron microscopic investigations on the location of rat liver ribosomal proteins S3a, S5, S6, S7, and S9 by means of antibody labeling. Biomed. Biochim. Acta 42: 705–723.
Maitra, U., Stringer, E.A., Chaudhuri, A. (1982). Initiation factors in protein biosynthesis. Ann. Rev. Biochem. 51: 869–900.
Nakashima, K., Darzynkiewicz, E., Shatkin, A.J. (1980). Proximity of mRNA 5′-region and 18S rRNA in eukaryotic initiation complexes. Nature 286: 226–230.
Nonomura, Y., Blobel, G., Sabatini, D. (1971). Structure of liver ribosomes studied by negative staining. J. Mol. Biol. 60: 303–324.
Nygård, O., Nika, H. (1982). Identification of RNA-protein cross-linking of ribosomal proteins located at the interface between the small and large subunit of mammalian ribosomes. EMBO J. 1: 357–362.
Nygård, O., Westermann, P. (1982a). Purification of protein synthesis initiation factor eIF-3 from rat liver microsomes by affinity chromatography on rRNA- cellulose. Biochim. Biophys. Acta 697: 263–269.
Nygård, O., Westermann, P. (1982b). Specific interaction of one subunit of eukaryotic initiation factor eIF-3 with 18S ribosomal RNA within the binary complex, eIF-3-small ribosomal subunit, as shown by cross-linking experiments. Nucl. Acids Res. 10: 1327–1334.
Nygård, O., Westermann, P. (1983). Structural organization of initiation complexes involving the eukaryotic protein synthesis initiation factors eIF-2 and eIF-3. In: Protein synthesis. Translational and posttranslational events, eds. Abraham, A.K. et al., The Humana Press, Clifton, NJ, pp. 3–21.
Nygård, O., Westermann, P., Hultin, T. (1980). Met-tRNAf is located in close proximity to the β-subunit of eIF-2 in the eukaryotic initiation complex [eIF-2. Met-tRNAf.GDPCP]. FEBS Lett. 113: 125–128.
Sargan, D.R., Gregory, S.P., Butterworth, P.H.W. (1982). A possible novel interaction between the 3′-end of 18S ribosomal RNA and the 5′-leader sequence of many eukaryotic messenger RNAs. FEBS Lett. 147: 133–136.
Sasisekharan, V., Sigler, P.B. (1965). An X-ray diffraction study of poly(A + U). J. Mol. Biol. 12: 296–298.
Schreier, M.H., Erni, B., Staehelin, T. (1977). Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors. J. Mol. Biol. 116: 727–753.
Schreier, M.H., Staehelin, T. (1973). Initiation of eukaryotic protein synthesis: [Met-tRNAf.40S ribosome] initiation complex catalysed by purified initiation factors in the absence of mRNA. Nat. New Biol. 242: 35–38.
Setyono, B., van Steeg, H., Voorma, H.O. (1984). Ultraviolet-crosslinking reveals specific affinity of eukaryotic initiation factors for Semliki Forest virus mRNA. Biochim. Biophys. Acta 782: 242–246.
Sonenberg, N., Morgan, M.A., Merrick, W.C., Shatkin, A.J. (1978). Polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA. Proc. Natl. Acad. Sci. USA 75: 4843–4847.
Stahl, J., Kobets, N.D. (1981). Affinity labeling of proteins at the mRNA binding site of rat liver ribosomes by an analogue of octauridylate containing an alkylating group attached to the 3′-end. FEBS Lett. 123: 269–272.
Sundkvist, I.C., Staehelin, T. (1975). Structure and function of free 40S ribosome subunits: characterization of initiation factors. J. Mol. Biol. 99: 401–418.
Svoboda, A.J., McConkey, E.H. (1978). Cross-linking of proteins to ribosomal RNA in Hela cell polysomes by sodium periodate. Biochem. Biophys. Res. Commun. 81: 1145–1152.
Takahashi, Y., Ogata, K. (1981). Ribosomal proteins cross-linked to natural mRNA by UY irradiation of rat liver polysomes. J. Biochem. 90: 1549–1552.
Terao, K., Uchiumi, T., Kobayashi, Y., Ogata, K. (1980). Identification of neighbouring protein pairs in the rat liver 40S ribosomal subunits cross-linked with dimethylsuberimidate. Biochim. Biophys. Acta 621: 72–82.
Thomas, A.A.M., Benne, R., Voorma, H.O. (1981). Initiation of eukaryotic protein synthesis. FEBS Lett. 128: 177–185.
Thomas, A., Goumans, H., Voorma, H.O., Benne, R. (1980). The mechanism of action of eukaryotic initiation factor 4C in protein synthesis. Eur. J. Biochem. 107: 39–45.
Thomas, N.S.B., Arnstein, H.R.V. (1984). Formation of a 22S mRNA • rRNA • protein complex during translation of globin mRNA. Eur. J. Biochem. 143: 27–33.
Tolan, D.R., Hershey, J.W.B., Traut, R.R. (1983). Cross-linking of eukaryotic initiation factor eIF-3 to the 40S ribosomal subunit from rabbit reticulocytes. Biochimie 65: 427–436.
Tolan, D.R., Traut, R.R. (1981). Protein topography of the 40S ribosomal subunit from rabbit reticulocytes shown by cross-linking with iminothiolane. J. Biol. Chem. 256: 10129–10136.
Trachsel, H., Erni, B., Schreier, M.H., Staehelin, T. (1977). Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors. J. Mol. Biol. 116: 755–767.
Trachsel, H., Staehelin, T. (1979). Initiation of mammalian protein synthesis. The multiple functions of the initiation factor eIF-3. Biochim. Biophys. Acta 565: 305–314.
Uchiumi, T., Terao, K., Ogata, K. (1981). Identification of neighbouring protein pairs cross-linked with dimethyl 3.3′dithiobispropionimidate in rat liver 40S ribosomal subunits. J. Biochem. 90: 185–193.
Westermann, P., Nygard, O. (1983). The spatial arrangement of the complex between eukaryotic initiation factor eIF-3 and 40S ribosomal subunit. Cross-linking between factor and ribosomal proteins. Biochim. Biophys. Acta 741: 103–108.
Westermann, P., Nygard, O. (1984). Cross-linking of mRNA to initiation factor eIF-3, 24kDa cap binding protein and ribosomal proteins SI, S3/3a, S6, and Sll within the 48S pre-initiation complex. Nucl. Acids Res. 12: 8887–8897.
Westermann, P., Heumann, W., Bommer, U.-A., Bielka, H., Nygård, 0., Hultin, T. (1979). Cross-linking of initiation factor eIF-2 to proteins of the small subunit of rat liver ribosomes. FEBS Lett. 97: 101–104.
Westermann, P., Gross, B., Bielka, H. (1980a). Neighbourhoods of proteins S2-S3, S3-S3a, S15-S15a, and S5-S25 within the small subunit of rat liver ribosomes. Acta Biol. Med. Germ. 39: 1147–1152.
Westermann, P., Nygård, O., Bielka, H. (1980b). The α- and γ-subunits of initiation factor eIF-2 can be cross-linked to 18S ribosomal RNA within the quarternary initiation complex, eIF-2 Met-tRNAf GDPCP • small ribosomal subunit. Nucl. Acids Res. 8: 3065–3071.
Westermann, P., Nygård, O., Bielka, H. (1981). Cross-linking of Met-tRNAf to eIF-2β? and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, eIF-2-GMPPCP-Met-tRNAf-small ribosomal subunit. Nucl. Acids Res. 9: 2387–2396.
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Westermann, P., Benndorf, R., Lutsch, G., Bielka, H., Nygård, O. (1986). Arrangement of Eukaryotic Initiation Factor 3 and Messenger RNA within Preinitiation Complexes. In: Hardesty, B., Kramer, G. (eds) Structure, Function, and Genetics of Ribosomes. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4884-2_37
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DOI: https://doi.org/10.1007/978-1-4612-4884-2_37
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