Structure of mammalian eIF3 in the context of the 43S preinitiation complex

Amedee des Georges, Vidya Dhote, Lauriane Kuhn, Christopher U. T. Hellen, Tatyana V. Pestova (), Joachim Frank () and Yaser Hashem ()
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Amedee des Georges: HHMI, Columbia University
Vidya Dhote: SUNY Downstate Medical Center
Lauriane Kuhn: CNRS
Christopher U. T. Hellen: SUNY Downstate Medical Center
Tatyana V. Pestova: SUNY Downstate Medical Center
Joachim Frank: HHMI, Columbia University
Yaser Hashem: CNRS, Architecture et Réactivité de l’ARN, Université de Strasbourg

Nature, 2015, vol. 525, issue 7570, 491-495

Abstract: Abstract During eukaryotic translation initiation, 43S complexes, comprising a 40S ribosomal subunit, initiator transfer RNA and initiation factors (eIF) 2, 3, 1 and 1A, attach to the 5′-terminal region of messenger RNA and scan along it to the initiation codon. Scanning on structured mRNAs also requires the DExH-box protein DHX29. Mammalian eIF3 contains 13 subunits and participates in nearly all steps of translation initiation. Eight subunits having PCI (proteasome, COP9 signalosome, eIF3) or MPN (Mpr1, Pad1, amino-terminal) domains constitute the structural core of eIF3, to which five peripheral subunits are flexibly linked. Here we present a cryo-electron microscopy structure of eIF3 in the context of the DHX29-bound 43S complex, showing the PCI/MPN core at ∼6 Å resolution. It reveals the organization of the individual subunits and their interactions with components of the 43S complex. We were able to build near-complete polyalanine-level models of the eIF3 PCI/MPN core and of two peripheral subunits. The implications for understanding mRNA ribosomal attachment and scanning are discussed.

Date: 2015
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DOI: 10.1038/nature14891

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