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.
journal_name
Proc Natl Acad Sci U S Aauthors
Tate WP,Beaudet AL,Caskey CTdoi
10.1073/pnas.70.8.2350subject
Has Abstractpub_date
1973-08-01 00:00:00pages
2350-5issue
8eissn
0027-8424issn
1091-6490journal_volume
70pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2020-08-11 00:00:00