A conserved HEAT domain within eIF4G Directs Assembly of the Translation Initiation Machinery

Joseph Marcotrigiano, Ivan B. Lomakin, Nahum Sonenberg, Tatyana V. Pestova, Christopher U.T. Hellen, Stephen K. Burley

Research output: Contribution to journalArticlepeer-review

158 Scopus citations

Abstract

The X-ray structure of the phylogenetically conserved middle portion of human eukaryotic initiation factor (eIF) 4GII has been determined at 2.4 Å resolution, revealing a crescent-shaped domain consisting of ten α helices arranged as five HEAT repeats. Together with the ATP-dependent RNA helicase eIF4A, this HEAT domain suffices for 48S ribosomal complex formation with a picornaviral RNA internal ribosome entry site (IRES). Structure-based site-directed mutagenesis was used to identify two adjacent features on the surface of this essential component of the translation initiation machinery that, respectively, bind eIF4A and a picornaviral IRES. The structural and biochemical results provide mechanistic insights into both cap-dependent and cap-independent translation initiation.

Original languageEnglish (US)
Pages (from-to)193-203
Number of pages11
JournalMolecular Cell
Volume7
Issue number1
DOIs
StatePublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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