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Isolation and Characterization of Eukaryotic Translation Initiation, Elongation and Termination Factors

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Post-transcriptional Control of Gene Expression

Part of the book series: NATO ASI Series ((ASIH,volume 97))

Abstract

Initiation factors were first isolated from mammalian cells. Using a cell-free system containing salt-washed rat ribosomal subunits, rabbit globin mRNA, charged tRNAs, ATP, GTP and purified translation elongation factors, Schreier, Erni and Staehelin (Schreier et al., 1977) defined a number of proteins from a rabbit ribosomal salt wash fraction, which were required to promote globin synthesis in vitro. These proteins were purified to homogeneity and shown to be required for the binding of initiator Met-tRNA and mRNA to ribosomes (Trachsel et al., 1977, for a review, see Hershey, 1991). These factors and factors isolated in other laboratories together with some of their properties are listed in Table 1.

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References

  • Böck A, Forchhammer K, Heider J, Baron C (1991) Selenoprotein synthesis: an expansion of the genetic code. Trends Biochem Sci 16:463–467.

    Article  PubMed  Google Scholar 

  • Browning KS, Ravel JM (1990) Determination of the amounts of the protein synthesis initiation and elongation factors in wheat germ. J Biol Chem 265:17967–17973.

    PubMed  CAS  Google Scholar 

  • Buwitt U, Flohr T, Bottger EC (1992) Molecular Cloning and Characterization of an Interferon Induced Human cDNA with Sequence Homology to a Mammalian Peptide Chain Release Factor. EMBO J ll(2):489–496.

    Google Scholar 

  • Coppard NJ, Clark FC (1991) 42Sp48 in previtellogenic Xenopus oocytes is structurally homologous to EF-1 alpha and may be a stage-specific elongation factor. J Cell Biol 112:237–243.

    Article  PubMed  CAS  Google Scholar 

  • Davydova EK, Ovchinnikov LP (1990) ADP-ribosylated elongation factor 2 (ADP-ribosyl-EF-2) is unable to promote translocation within the ribosome. Febs Lett 261:350–352.

    Article  PubMed  CAS  Google Scholar 

  • Dever TE, Feng L, Wek RC, Cigan AM, Donahue TF, Hinnebusch AG (1992) Phosphorylation of initiation factor 2a by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585–596.

    Article  PubMed  CAS  Google Scholar 

  • Didichenko SA, Ter-Avanesyan M, Smirnov V (1991) Ribosome-bound EF-1 alpha-like protein of yeast Saccharomyces cerevisiae. Eur J Biochem 198:705–711.

    Article  PubMed  CAS  Google Scholar 

  • Donahue TF, Cigan AM, Pabich EK, Castillo Valavicius B (1988) Mutations at a Zn(II) finger motif in the yeast eIF-2ß gene alter ribosomal start-site selection during the scanning process. Cell 54:621–632.

    Article  PubMed  CAS  Google Scholar 

  • Gulyas KD, Donahue TF (1992) SSL2, a suppressor of a stem-loop mutation in the HIS4 leader encodes the yeast homolog of human ERCC-3. Cell 69:1031–1042.

    Article  PubMed  CAS  Google Scholar 

  • Hanic-Joyce PJ, Singer RA, Johnston GC (1987) Molecular characterization of the yeast PRT1 gene in which mutations affect translation initiation and regulation of cell proliferation. J Biol Chem 262:2845–2851.

    PubMed  CAS  Google Scholar 

  • Hershey JWB (1989) Protein phosphorylation controls translation rates. J Biol Chem 264:20823–20826.

    PubMed  CAS  Google Scholar 

  • Hershey JWB (1991) Translational control in mammalian cells. Annu. Rev. Biochem. 60:717–755.

    Article  PubMed  CAS  Google Scholar 

  • Keierleber C, Wittekind M, Qin S, McLaughlin CS (1986) Isolation and characterization of PRT1, a gene required for the initiation of protein biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol 6:4419–4424.

    PubMed  CAS  Google Scholar 

  • Kozak M (1991) An analysis of vertebrate mRNA sequences: Intimations of translational control. J Cell Biol 115:887–903.

    Article  PubMed  CAS  Google Scholar 

  • Linder P, Lasko PF, Leroy P, Nielsen PJ, Nishi K, Schnier J, Slonimsky PP (1989) Birth of the D-E-A-D box. Nature 337:121–122.

    Article  PubMed  CAS  Google Scholar 

  • Marcus A (1970) Tobacco mosaic virus ribonucleic acid-dependent amino acid incorporation in a wheat embryo system. J Biol Chem 245:955–961.

    PubMed  CAS  Google Scholar 

  • Milburn SC, Hershey JWB, Davies MV, Kelleher K, Kaufman RJ (1990) Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif. EMBO J 9:2783–2790.

    PubMed  CAS  Google Scholar 

  • Mueller PP, Trachsel H (1990) Translation and regulation of translation in the yeast Saccharomyces cerevisiae. Eur J Biochem 191:257–261.

    Article  CAS  Google Scholar 

  • Nielsen PJ, Trachsel H (1988) The mouse protein synthesis initiation factor 4A gene family includes two related functional genes which are differentially expressed. EMBO J 7:2097–2105.

    PubMed  CAS  Google Scholar 

  • Noller HF, Hoffarth V, Zimniak L (1992) Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures. Science 256(5062):1416–1419.

    Article  PubMed  CAS  Google Scholar 

  • Pathak VK, Nielsen PJ, Trachsel H, Hershey JWB (1988) Structure of the ß-subunit of translation initiation factor eIF-2. Cell 54:633–639.

    Article  PubMed  CAS  Google Scholar 

  • Riis B, Merrick WC (1990) Eukaryotic protein elongation factors. Trends Biochem Sci 15:420–424.

    Article  PubMed  Google Scholar 

  • Ryazanov AG, Shestakova E A, Natapov PG (1988) Phosphorylation of EF-2 by EF-2 kinase affects rate of translation. Nature 334:170–173.

    Article  PubMed  CAS  Google Scholar 

  • Schnier J (1991) Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast S. cerevisiae. Mol Cell Biol 11:3105–3114.

    PubMed  CAS  Google Scholar 

  • Schreier MH, Erni B, Staehelin T (1977) Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors. J Mol Biol 116:727–753.

    CAS  Google Scholar 

  • Shepherd JCW, Gehring WJ (1989) Fruit flies with additional expression of the elongation factor EF-la live longer. Proc Natl Acad Sci USA 86:7520–7521.

    Article  PubMed  CAS  Google Scholar 

  • Sonenberg N (1991) Picornavirus RNA translation continues to surprise. Trends in Genetics 7:105–106.

    Article  PubMed  CAS  Google Scholar 

  • Trachsel H, Erni B, Schreier MH, 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.

    CAS  Google Scholar 

  • Yoon H, Donahue TF (1992) The Suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNAmet recognition of the start codon. Mol Cell Biol 12:248–260.

    PubMed  CAS  Google Scholar 

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© 1996 Springer-Verlag Berlin Heidelberg

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Trachsel, H. (1996). Isolation and Characterization of Eukaryotic Translation Initiation, Elongation and Termination Factors. In: Resnekov, O., von Gabain, A. (eds) Post-transcriptional Control of Gene Expression. NATO ASI Series, vol 97. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60929-9_14

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  • DOI: https://doi.org/10.1007/978-3-642-60929-9_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-64609-6

  • Online ISBN: 978-3-642-60929-9

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