Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation

Mikkel A. Algire, David Maag, Jon R. Lorsch

Research output: Contribution to journalArticle

Abstract

Irreversible GTP hydrolysis by eIF2 is a critical step in translation initiation in eukaryotes because it is thought to commit the translational machinery to assembling the ribosomal complex at the selected point in the mRNA. Our quantitative analysis of the steps and interactions involved in activating GTP hydrolysis by eIF2 during translation initiation in vitro indicates that a structural rearrangement in the 43S preinitiation complex activates it to become fully competent to hydrolyze GTP. Contrary to the prevailing model, release of inorganic phosphate after GTP hydrolysis by eIF2, not hydrolysis itself, is controlled by recognition of the AUG codon. Release of Pi, which makes GTP hydrolysis irreversible, appears to be controlled by the AUG-dependent dissociation of eIF1 from the preinitiation complex.

Original languageEnglish (US)
Pages (from-to)251-262
Number of pages12
JournalMolecular Cell
Volume20
Issue number2
DOIs
StatePublished - Oct 28 2005

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Guanosine Triphosphate
Hydrolysis
Eukaryota
Codon
Phosphates
Messenger RNA

ASJC Scopus subject areas

  • Molecular Biology

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Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. / Algire, Mikkel A.; Maag, David; Lorsch, Jon R.

In: Molecular Cell, Vol. 20, No. 2, 28.10.2005, p. 251-262.

Research output: Contribution to journalArticle

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