Functional Role and Biochemical Properties of Yeast Peptide Elongation Factor 3 (EF-3)

  • Masazumi Miyazaki
  • Masahiro Uritani
  • Yoshihisa Kitaoka
  • Kazuko Ogawa
  • Hideto Kagiyama
Conference paper
Part of the NATO ASI Series book series (volume 49)

Abstract

The eukaryotic peptide elongation cycle is well known to be driven by the two complementary factors EF-lα and EF-2, functionally analogous to the bacterial EF-Tu and EF-G, respectively, and the two GTP hydrolysis steps catalyzed by those factors have been considered to be essential for the cycle to run (Kaziro, 1978; Moldave, 19 85). On yeast ribosomes, however, the elongation process additionally requires the third soluble factor, which was found by Skogerson and collaborators (1976, 1977) using poly- (U)-dependent protein synthesis systems and designated as EF-3. Inhibition experiments with monoclonal (Hutchison et al., 1984) and polyclonal (Dasmahapatra and Chakraburtty, 1981; Miyazaki and Kagi-yama, to be published) antibody raised against EF-3 demonstrated that the factor was essential for the elongation phase in the translation of natural mRNA as well as poly(U). A temperature- sensitive yeast mutant producing a thermolabile EF-3 was blocked in the elongation cycle at a non-permissive temperature, indicating the factor indispensable for the in vivo translation (Herrera et al., 1984; Kamath and Chakraburtty, 1986b; Qin et al., 1987).

Keywords

Sugar Hydrolysis Cysteine Vanadate Thiol 

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References

  1. Chakraburtty K, Kamath A(1988) Protein synthesis in yeast. Int J Biochem vol 120: 581–590Google Scholar
  2. Dasmahapatra B, Chakraburtty K(1981) Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae. J Biol Chem 256: 9999–10004Google Scholar
  3. Herrera F, Martinez JA, Moreno N, Sadnik I, McLaughlin CS, Fein- berg B, Moldave K(1984) Identification of an altered elonga-tion factor in temperature-sensitive mutants ts7,-14 of Saccharomyces cerevisiae. J Biol Chem 259: 14347–14349Google Scholar
  4. Hutchison JS, Feinberg B, Rothwell TC, Moldave K(1984) Monoclonal antibody specific for yeast elongation factor 3. Biochemistry 23: 3055–3063Google Scholar
  5. Kamath A, Chakraburtty K (1986a)Purification of elongation factor 3 from temperature-sensitive mutant 13-06 of the yeast Saccharomyces cerevisiae. J Biol Chem 261: 12596–12598Google Scholar
  6. Kamath A, Chakraburtty K(1986b)Identification of an altered elongation in the thermolabile mutants of the yeast Saccharomy ces cerevisiae. J Biol Chem 261: 12593–12595Google Scholar
  7. Kaziro Y (1978) The role of guanosine 51-triphosphate in polypeptide chain elongation. Biochim Biophys Acta 505: 95–127PubMedGoogle Scholar
  8. Miyazaki M, Uritani M(1985) Studies on the occurrence of elongation factor 3 in lower eukaryotes other than yeasts. 13th Int Congr Biochem Abstracts p60Google Scholar
  9. Miyazaki M, Uritani M, Kagiyama H(1988) The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes. J Biochem (Tokyo) 104: 445–450Google Scholar
  10. Miyazaki M, Kagiyama H (to be published) Soluble factor requirements for the Tetrahymena ribosomes and the ribosomal ATPase as an counterpart of yeast elongation factor 3 (EF-3). J Biochem (Tokyo)Google Scholar
  11. Moldave K(1985) Eukaryotic protein synthesis. Ann Rev Biochem 54: 1109–1149Google Scholar
  12. Qin S, Moldave K, McLaughlin CS (1987) Isolation of the yeast gene encoding elongation factor 3 for protein synthesis. J Biol Chem 262: 7802–7807PubMedGoogle Scholar
  13. Qin S, Xie A, Christina M, Bonato M, McLaughlin CS (1990) Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae. J Biol Chem 265: 1903–1912PubMedGoogle Scholar
  14. Skogerson L, Wakatama E (1976) A ribosome-dependent GTPase from yeast distinct from elongation factor 2. Proc Natl Acad Sci US 73: 73–76CrossRefGoogle Scholar
  15. Skogerson L, Engelhardt D (1977) Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes. J Biol Chem 252: 1471–1475PubMedGoogle Scholar
  16. Skogerson L (1979) Separation and characterization of yeast elongation factors. In; Moldave K and Grossman L(ed) Methods in enzymology vol LX Academic Press, New York, p6 76Google Scholar
  17. Uritani M, Miyazaki M (1985) Interaction of yeast polypeptide chain elongation factor 3 (EF-3) with different nucleotides. Nucleic Acids Res Symp Ser No 16: 229–232Google Scholar
  18. Uritani M, Miyazaki M (1988a) Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts. J Biochem (Tokyo) 103: 522–530Google Scholar
  19. Uritani M, Miyazaki M (1988b) Role of yeast peptide elongation factor 3 (EF-3) at the AA-tRNA binding step. J Biochem 104: 118–126PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • Masazumi Miyazaki
    • 1
  • Masahiro Uritani
    • 1
  • Yoshihisa Kitaoka
    • 1
  • Kazuko Ogawa
    • 1
  • Hideto Kagiyama
    • 1
  1. 1.Department of Molecular Biology School of ScienceNagoya UniversityNagoyaJapan

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