PMID:15985150

Citation	Zavialov, AV, Hauryliuk, VV and Ehrenberg, M (2005) Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs. J. Biol. 4:9
Abstract	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 recent model, EF-G operates like a 'motor protein' and drives translocation of the peptidyl-tRNA after GTP hydrolysis. In both the classical and motor protein models, GDP-to-GTP exchange is assumed to occur spontaneously on 'free' EF-G even in the absence of a guanine-nucleotide exchange factor (GEF).
Links	PubMed PMC1175996 Online version:10.1186/jbiol24
Keywords	Escherichia coli/genetics; Escherichia coli/metabolism; Guanine Nucleotides/genetics; Guanine Nucleotides/metabolism; Models, Biological; Peptide Elongation Factor G/genetics; Peptide Elongation Factor G/metabolism; Protein Biosynthesis; RNA, Transfer, Amino Acyl/metabolism; Ribosomes/genetics; Ribosomes/metabolism
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