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• W2030355192 abstract "Release of formylmethionine from the reticulocyte ribosomal substrate, f[(3)H]Met-tRNA.ribosome, is promoted by reticulocyte release factor (RF). The initial rate of this reaction is stimulated by GTP but inhibited by GDPCP. Formation of an RF.UA[(3)H]A(2).ribosome complex is a measure of the binding of reticulocyte RF to the ribosome, and the recovery of this complex is increased by GDPCP and, to a lesser extent, GTP. These studies suggest that GTP is involved in the initial association of RF with the ribosome and that hydrolysis of the gamma-phosphate of the guanine nucleotide is required at a subsequent rate-limiting step. The ribosomal-dependent fMet-tRNA hydrolysis and GTPase activities of reticulocyte RF are inhibited when elongation factor (EF)-2 is bound to the respective ribosomal substrate in the presence of fusidic acid and GDP. When EF-G is bound to the f[(3)H]Met-tRNA.AUG.ribosome substrate with fusidic acid and GDP, the fMet-tRNA hydrolysis activity of Escherichia coli RF-1 and RF-2 is also inhibited. The binding of reticulocyte RF and E. coli RF-1 or RF-2 to their respective ribosomes is prevented when fusidic acid.EF-2/EF-G.GDP.ribosome complexes are used." @default.
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• W2030355192 date "1973-08-01" @default.
• W2030355192 modified "2023-09-28" @default.
• W2030355192 title "Influence of Guanine Nucleotides and Elongation Factors on Interaction of Release Factors with the Ribosome" @default.
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• W2030355192 doi "https://doi.org/10.1073/pnas.70.8.2350" @default.
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