A ribosome-dependent GTPase from yeast distinct from elongation factor 2

Proc Natl Acad Sci U S A. 1976 Jan;73(1):73-6. doi: 10.1073/pnas.73.1.73.

Abstract

Three proteins required for poly(U)-directed polyphenylalanine synthesis have been separated from yeast. Two of the factors correspond to the elongation factors 1 and 2 described for other eukaryotic systems, according to the criteria of phenylalanyl-tRNA binding and diphtheria toxin-catalyzed ADP-ribosylation. The third protein, while absolutely required for polyphenylalanine synthesis, was a more active ribosome-dependent GTPase than elongation factor 2.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Cell-Free System
  • Diphtheria Toxin / metabolism
  • Fusidic Acid / pharmacology
  • GTP Phosphohydrolase-Linked Elongation Factors / antagonists & inhibitors
  • GTP Phosphohydrolase-Linked Elongation Factors / metabolism*
  • Peptide Chain Elongation, Translational*
  • Peptide Elongation Factors / isolation & purification*
  • Phenylalanine / metabolism
  • Phosphoric Monoester Hydrolases / metabolism*
  • Poly U / metabolism
  • RNA, Transfer / metabolism
  • Ribosomes / metabolism*
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Diphtheria Toxin
  • Peptide Elongation Factors
  • Poly U
  • Phenylalanine
  • Fusidic Acid
  • Adenosine Diphosphate
  • RNA, Transfer
  • Phosphoric Monoester Hydrolases
  • GTP Phosphohydrolase-Linked Elongation Factors