Inhibition by Elongation Factor EF G of Aminoacyl-tRNA Binding to Ribosomes
نویسندگان
چکیده
منابع مشابه
Inhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.
Elongation factor G (EF G), bound to ribosomes either with GMPPCP or with fusidic acid and GDP, inhibits elongation factor Tu (EF Tu)-dependent binding of Phe-tRNA on the ribosome-poly(U) complex and binding of Ala-tRNA on the initiation complex formed with RNA from bacteriophage R17; GTP hydrolysis associated with Phe-tRNA binding is also inhibited. Moreover, nonenzymic binding of Phe-tRNA at ...
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Siomycin, a peptide antibiotic that interacts with the 50S ribosomal subunit and inhibits binding of factor G, is shown also to inhibit binding of aminoacyl-tRNA; however, it does not impair binding of fMet-tRNA and completion of the initiation complex. Moreover, unlike other inhibitors of aminoacyl-tRNA binding (tetracycline, sparsomycin, and streptogramin A), siomycin completely abolishes the...
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Ribosomes complexed with poly(U) and Phe-transfer RNA (tRNA) have been examined for their ability to interact with elongation factor G (EF-G). It is shown that PhetRNA, bound to ribosomes either at 6 mM Mg2+ in the presence of elongation factor Tu and GTP or at 20 rn~ Mg2+ in the absence of these compounds, strongly inhibits (50 to 90%) the binding of EF-G, as measured by the formation of eithe...
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Here, we examine tRNA-aminoacyl synthetase (ARS) localization in protein synthesis. Proteomics reveals that ten of the twenty cytosolic ARSs associate with ribosomes in sucrose gradients: phenylalanyl-RS (FRS), and the 9 ARSs that form the multi-ARS complex (MSC). Using the ribopuromycylation method (RPM) for localizing intracellular translation, we show that FRS and the MSC, and to a lesser ex...
متن کاملInteraction of eukaryote elongation factor EF 1 with guanosine nucleotides and aminoacyl-tRNA.
Evidence for two species of elongation factor 1 (EF 1(A) and EF 1(B)) from calf brain has been obtained by molecular sieve chromatography on Sephadex G-150. A high molecular weight form, EF 1(A), interacts with GTP to form an EF 1(A)-GTP complex. GDP also reacts with EF 1, but unlike the reaction with GTP, an EF 1(B)-GDP complex is formed that contains a lower molecular weight and labile specie...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1972
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.69.3.733