A ribosome-dependent GTPase from yeast distinct from elongation factor 2.
- 1 January 1976
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (1) , 73-76
- https://doi.org/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.Keywords
This publication has 20 references indexed in Scilit:
- Structure and Function of the Bacterial RibosomeAnnual Review of Biochemistry, 1972
- Hydrolysis of guanosine 5'-triphosphate associated wh binding of aminoacyl transfer ribonucleic acid to ribosomes.1969
- Fusidic Acid: Inhibition of Factor T 2 in Reticulocyte Protein SynthesisScience, 1969
- Adenosine Diphosphoribosylation of Aminoacyl Transferase II by Diphtheria ToxinCold Spring Harbor Symposia on Quantitative Biology, 1969
- Purification and Properties of Factor GCold Spring Harbor Symposia on Quantitative Biology, 1969
- Stepwise synthesis of a tripeptide.Proceedings of the National Academy of Sciences, 1968
- Translocase activity in the aminoacyl transferase II fraction from rat liverBiochemical and Biophysical Research Communications, 1968
- Diphtheria Toxin-dependent Adenosine Diphosphate Ribosylation of Aminoacyl Transferase II and Inhibition of Protein SynthesisJournal of Biological Chemistry, 1968
- Comparison of amino acid polymerization factors isolated from rat liver and rabbit reticulocytesArchives of Biochemistry and Biophysics, 1968
- STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXINThe Journal of Experimental Medicine, 1967