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Nat Struct Mol Biol. 2006 Mar;13(3):234-41. Epub 2006 Feb 26.

The hybrid state of tRNA binding is an authentic translation elongation intermediate.

Author information

1
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Abstract

The GTPase elongation factor (EF)-G is responsible for promoting the translocation of the messenger RNA-transfer RNA complex on the ribosome, thus opening up the A site for the next aminoacyl-tRNA. Chemical modification and cryo-EM studies have indicated that tRNAs can bind the ribosome in an alternative 'hybrid' state after peptidyl transfer and before translocation, though the relevance of this state during translation elongation has been a subject of debate. Here, using pre-steady-state kinetic approaches and mutant analysis, we show that translocation by EF-G is most efficient when tRNAs are bound in a hybrid state, supporting the argument that this state is an authentic intermediate during translation.

PMID:
16501572
PMCID:
PMC1687179
DOI:
10.1038/nsmb1060
[Indexed for MEDLINE]
Free PMC Article

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