Abstract
“Translational initiation” consists of an ill-defined number of interrelated steps preceding the formation of the first peptide bond. In Escherichia coli, in addition to mRNA, fmet-tRNA, and ribosomal subunits, initiation involves and requires three factors (IF-1, IF-2, and IF-3) and a GTP molecule. Fundamental problems concerning how the mRNA initiation region and the initiator tRNA are recognized, the role played by the initiation factors and GTP, and important mechanistic aspects, including the mechanism by which the factors are ejected from ribosomes, still remain open.
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References
Boileau, G., Butler, P., Hershey, J.W.B., Traut, R.R. (1983). Direct cross-links between initiation factors 1,2 and 3 and ribosomal proteins promoted by 2-imino- thiolane. Biochemistry 22: 3162–3170.
Brauer, D., Wittmann-Liebold, B. (1977). The primary structure of IF 3 from E. coli. FEBS Lett. 79: 269–275.
Bruhns, J. (1980). Struktur-Funktionsbeziehungen in den Initiationsfaktoren IF1 und IF 3 aus E. coli: Einfluß der Tyrosine auf die ribosomale Bindung und die biologische Aktivität. Ph.D. Dissertation. Technical University, Berlin.
Bruhns, J., Gualerzi, C. (1980). Role of tyrosine residues in ribosomal binding and functional activity of IF 3. Biochemistry 19: 1670–1676.
Chaires, J.B., Pande, C, Wishnia, A. (1981). The effect of IF 3 on E. coli ribosomal subunit association kinetics. J. Biol. Chem. 256: 6600–6607.
Goss, D.J., Parkhurst, L.J., Wahba, A.J. (1982). Kinetic studies on the interaction of chain initiation factor 3 with 70S E. coli ribosomes and subunits. J. Biol. Chem. 257: 10119–10127.
Gottlieb, M., Davis, B.D. (1975). The irreversible step in formation of initiation complexes of E. coli. Biochemistry 14: 1047–1051.
Gualerzi, C., Pon, C. (1981). Protein biosynthesis in prokaryotic cells: mechanism of 30S initiation complex formation in Escherichia coli. In: Structural aspects of recognition and assembly in biological macromolecules, vol. II, ed. Balaban, M. ISS, Rehovot, pp. 805–826.
Gualerzi, C., Risuleo, G., Pon, C. (1977). Initial rate kinetic analysis of the mechanism of initiation complex formation and the role of IF 3. Biochemistry 16: 1684–1689.
Gualerzi, C., Risuleo, G., Pon, C. (1979). Mechanism of the spontaneous and IF3-induced dissociation of 30 S aminoacyl-tRNA polynucleotide ternary complexes. J. Biol. Chem. 254: 44–49.
Jay, G., Kaempfer, R. (1975). Initiation of protein synthesis. Binding of messenger RNA. J. Biol. Chem. 250: 5742–5748.
Kimura, M., Ernst, H., Appelt, K. (1983). The primary structure of IF 3 from Bacillus stearothermophilus. FEBS Lett. 160: 78–81.
Kyte, J., Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105–132.
Lammi, M., Paci, M., Pon, C.L., Gualerzi, C. (1982). Biochemical and 1H-NMR spectroscopic study on the involvement of the His residue in the interaction between IF 3 and ribosomes. Biochem. Internat. 5: 429–436.
Miller, M.J., Wahba, A.J. (1973). Chain initiation factor 2. Purification and properties of two species from E. coli MRE600. J. Biol. Chem. 248: 1084–1090.
Noll, M., Hapke, B., Noll, H. (1973). Structural dynamics of bacterial ribosomes. II. Preparation and characterization of ribosomes and subunits active in the translation of natural mRNA. J. Mol. Biol. 80: 519–530.
Noll, M., Noll, H. (1976). Structural dynamics of bacterial ribosomes. V. Mg- dependent dissociation of tight couples into subunits: measurements of dissociation constants and exchange rates. J. Mol. Biol. 105: 111–130.
Ohsawa, H., Gualerzi, C. (1981). Identification of a lysine residue in the ribosomal binding site of IF 3 by site-specific chemical modification with pyridoxal phosphate. J. Biol. Chem. 256: 4905–4912.
Paci, M., Pon, C., Gualerzi, C. (1983). High resolution 1-NMR study of the interaction between IF1 and 30S ribosomal subunits. EMBO J. 2: 521–526.
Paci, M., Pon, C., Gualerzi, C. (1985). The interaction between IF 3 and 30S ribosomal subunits studied by high-resolution 1N-NMR spectroscopy. J. Biol. Chem. 260: 887–892.
Paci, M., Pon, C., Lammi, M., Gualerzi, C. (1984). Characterization of IF 3 by high resolution 1H-NMR spectroscopy. J. Biol. Chem. 259: 9628–9634.
Parmeggiani, A., Sander, G. (1981). Properties and regulation of the GTPase activities of EF-Tu and G, and of IF2. Mol. Cell. Biochem. 35: 129–158.
Pawlik, R.T., Littlechild, J., Pon, C., Gualerzi, C. (1981). Purification and properties of E. coli translational initiation factors. Biochem. Internat. 2: 421–428.
Petersen, H.U., Røll, T., Grunberg-Manago, M., Clark, B.F.C. (1979). Specific interaction of IF 2 of E. coli with fMet-tRNAfmet. Biochem. Biophys. Res. Commun. 91: 1068–1074.
Pon, C., Cannistraro, S., Giovane, A., Gualerzi, C. (1982a). Environment of the Cys residue and evidence for a hydrophobic region in IF 3 by fluorescence and ESR spectroscopy. Arch. Biochem. Biophys. 217: 47–57.
Pon, C., Gualerzi, C. (1984). Mechanism of protein biosynthesis in prokaryotic cells. Effect of IF 1 on the initial rate of 30S initiation complex formation. FEBS Lett. 175: 203–207.
Pon, C.L., Paci, M., Pawlik, R.T., Gualerzi, C.O. (1985). Biochemical and biophysical characterization of the interaction between IF 2 and guanosine nucleotides. J. Biol. Chem. 260: 8918–8924.
Pon, C.L., Pawlik, R.T., Gualerzi, C. (1982b). The topographical localization of IF 3 on E. coli 30S ribosomal subunits as a clue to its way of functioning. FEBS Lett. 137: 163–167.
Pon, C., Wittmann-Liebold, B., Gualerzi, C. (1979). Elucidation of the primary structure of IF1. FEBS Lett. 101: 157–160.
Sacerdot, C., Dessen, P., Hershey, J.W.B., Plumbridge, J.A., Grunberg-Manago, M. (1984). Sequence of the IF2 gene: unusual protein features and homologies with elongation factors. Proc. Natl. Acad. Sci. USA 81: 7787–7791.
Sacerdot, C., Fayat, G., Dessen, P., Springer, M., Plumbridge, J.A., Grunberg-Manago, M., Blanquet, S. (1982). Sequence of a 1.26 kb DNA fragment containing the structural gene for E. coli IF 3: presence of an AUU initiator codon. EMBO J. 1: 311–315.
Schleich, T., Wickstrom, E., Twombly, K., Schmidt, B., Tyson, R.W. (1980). Circular dichroism study of E. coli IF 3 binding to nucleic acids. Biochemistry 19: 4486–4492.
Stormo, G.D., Schneider, T.D., Gold, L.M. (1982). Characterization of translational initiation sites in E. coli. Nucl. Acids Res. 10: 2971–2996.
Travers, A.A., Debenham, P.G., Pongs, O. (1980). Translational initiation factor 2 alters transcriptional selectivity of E. coli ribonucleic acid polymerase. Biochemistry 19: 1651–1656.
van der Hofstad, G.A.J.M., Buitenhek, A., Bosch, L., Voorma, H.O. (1978). IF 3 and the binary complex between IF 2 and fMet-tRNA are mutually exclusive on the 30S ribosomal subunit. Eur. J. Biochem. 89: 213–220.
van der Hofstad, G.A.J.M., Foekens, J.A., Bosch, L., Voorma, H.O. (1977). Cooperative effects of initiation factors and fMet-tRNA in the formation of the 40S initiation complex. Eur. J. Biochem. 77: 69–75.
Weiel, J., Hershey, J.W.B. (1982). The binding of fluorescein-labeled protein synthesis initiation factor 2 to E. coli 30S ribosomal subunits determined by fluorescence polarization. J. Biol. Chem. 257: 1215–1220.
Wintermeyer, W., Gualerzi, C. (1983). Effect of E. coli initiation factors on the kinetics of Af-AcPhe-tRNAPhe binding to 30S ribosomal subunits. A fluorescence stopped-flow study. Biochemistry 22: 690–694.
Wishnia, A., Boussert, A., Graffe, M., Dessen, P., Grunberg-Manago, M. (1975). Kinetics of the reversible association of ribosomal subunits: stopped-flow studies of the rate law and of the effect of Mg2 +. J. Mol. Biol. 93: 499–515.
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Gualerzi, C.O., Pon, C.L., Pawlik, R.T., Canonaco, M.A., Paci, M., Wintermeyer, W. (1986). Role of the Initiation Factors in Escherichia coli Translational Initiation. 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_36
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DOI: https://doi.org/10.1007/978-1-4612-4884-2_36
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