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

Silke Dorner, Julie L. Brunelle, Divya Sharma, Rachel Green

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)234-241
Number of pages8
JournalNature Structural and Molecular Biology
Volume13
Issue number3
DOIs
StatePublished - Mar 1 2006

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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