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. 1973 Dec;70(12 Pt 1-2):3561–3565. doi: 10.1073/pnas.70.12.3561

The Interaction of Elongation Factor G with N-Acetylphenylalanyl Transfer RNA·Ribosme Complexes

Juan Modolell 1, Bartolomé Cabrer 1, David Vázquez 1
PMCID: PMC427280  PMID: 4519646

Abstract

N-Acetyl-Phe-tRNA, nonenzymically bound to the acceptor site of Escherichia coli ribosomes, readily undergoes translocation in the presence of elongation factor (EF)-G and GTP. The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP·EF-G·fusidic acid·ribosome complex or the 5′-guanylylmethylenediphosphonate·EF-G·ribosome complex. Deacylation with puromycin of the donor site-bound N-acetyl-Phe-tRNA reverses these inhibitions, even though the tRNAPhe moiety remains bound to the ribosme. These results suggest that ribosomes complexed with messenger RNA and peptidyl-tRNA may be restricted in their ability to interact with EF-G to that part of the elongation cycle when peptidyl-tRNA is in the acceptor site, and deacylated tRNA in the donor site. Deacylation of the donor site-bound peptidyl-tRNA associated with peptide bond formation may control the interaction of EF-G with the ribosome.

Keywords: translocation, GTPase, EF-Tu, ribosomal sites, fusidic acid

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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