Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes.
L Skogerson,D Engelhardt +1 more
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TL;DR: The data suggest that the yeast EF-3 may be a loosely bound ribosomal protein which is not required for a specific step in the elongation cycle but is involved in the coordination of the partial reactions required for polymerization.
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About: This article is published in Journal of Biological Chemistry. The article was published on 25 Feb 1977. and is currently open access. The article focuses on the topics: Elongation factor & Yeast.
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Citations
Comparative Analysis of Ribosome‐Associated Adenosinetriphosphatase (ATPase) from Pig Liver and the ATPase of Elongation Factor 3 from Saccharomyces cerevisiae
TL;DR: Four lines of evidence indicate that yeast EF-3 ATPase is functionally distinct from pig liver ribosome associated ATPase, and reflects a direct correlation between EF- 3 ATPase and the functional state of the ribosomes.
28
Candida albicans and three other Candida species contain an elongation factor structurally and functionally analogous to elongation factor 3
TL;DR: A cell-free poly(U)-dependent translation elongation system from Candida albicans is ATP-dependent due to the presence of an elongation factor 3 (EF3-like activity) and was used to screen a selection of Candida species.
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Yeast as a sensor of factors affecting the accuracy of protein synthesis.
Louis Valente,Terri Goss Kinzy +1 more
TL;DR: The yeast Saccharomyces cerevisiae has proven an ideal system to study translational fidelity by integrating genetic approaches with biochemical analysis and the ways studies in yeast have contributed to understanding of the roles translation factors and the ribosome play in assuring the accuracy of protein synthesis.
27
ATPase strongly bound to higher eukaryotic ribosomes.
TL;DR: The hydrolysis of ATP is likely to be involved in the mechanism of tRNA binding to the A site of the 80 S ribosome, and the ribosomal ATPase seems to be similar to EF-3 found in fungi.
27
Yeast Elongation Factor 3: Structure and Function
TL;DR: The deduced amino acid sequence of EF-3 has revealed the presence of duplicated ATP-binding cassettes similar to those present in the membrane associated transporters and the existence of functional homologs ofEF-3 in higher eukaryotes is still an open question.
26
References
Requirement of an Escherichia coli 50 S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate.
TL;DR: Escherichia coli ribosomes were made deficient in a 50 S ribosomal protein component by treatment with ethanol and NH4Cl and their ability to carry out a number of partial reactions involved in polypeptide synthesis was examined.
363
Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis.
Corinne C. Sherton,Ira G. Wool +1 more
TL;DR: The number of proteins in rat liver ribosome was determined by two-dimensional polyacrylamide gel electrophoresis and it is estimated that eukaryotic ribosomes contain between 68 and 72 different proteins.
252
Comparison of amino acid polymerization factors isolated from rat liver and rabbit reticulocytes
Luciano Felicetti,Fritz Lipmann +1 more
TL;DR: Using preliminary ammonium sulfate fractionation followed by calcium phosphate adsorption and elution, two complementary fractions, T 1 and T 2 , analogous to Schweet's TF-1 and TF-2, were obtained from liver as well as reticulocytes.
115
A ribosome-dependent GTPase from yeast distinct from elongation factor 2
TL;DR: Three proteins required for poly(U)-directed polyphenylalanine synthesis have been separated from yeast and it was found that one was a more active ribosome-dependent GTPase than elongation factor 2.
91