Elongation factor G initiates translocation through a power stroke
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چکیده
منابع مشابه
Elongation factor G initiates translocation through a power stroke.
During the translocation step of prokaryotic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (GTPase), binds to the ribosomal PRE-translocation (PRE) complex and facilitates movement of transfer RNAs (tRNAs) and messenger RNA (mRNA) by one codon. Energy liberated by EF-G's GTPase activity is necessary for EF-G to catalyze rapid and precise translocation. Whether this e...
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BACKGROUND During the translation of mRNA into polypeptide, elongation factor G (EF-G) catalyzes the translocation of peptidyl-tRNA from the A site to the P site of the ribosome. According to the 'classical' model, EF-G in the GTP-bound form promotes translocation, while hydrolysis of the bound GTP promotes dissociation of the factor from the post-translocation ribosome. According to a more rec...
متن کاملConformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation
The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on the ribosome after peptide bond formation. Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements during translocation, high-resolution structures exist for essentially only one conformation of EF-G in complex with the ribosome. Here, we report fou...
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Translocation, a coordinated movement of two tRNAs together with mRNA on the ribosome, is catalyzed by elongation factor G (EF-G). The reaction is accompanied by conformational rearrangements of the ribosome that are, as yet, not well characterized. Here, we analyze those rearrangements by restricting the conformational flexibility of the ribosome by antibiotics binding to specific sites of the...
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The role of GTP in the translocation reaction catalyzed by elongation factor G (EF-G) has been investigated. The addition of EF-G and GTP to a poly(U)-ribosome complex having deacylated tRNA in the P site and N-acetykliphenylalanyl-tRNA in the A site (Complex II) results in the shift of N-acetyldiphenylalanyl-tRNA from the A to the P site of ribosomes with a concomitant release of tRNA from the...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2016
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1602668113