eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core

Yuliya Gordiyenko, Carla Schmidt, Martin D. Jennings, Dijana Matak-Vinkovic, Graham D. Pavitt () and Carol V. Robinson ()
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Yuliya Gordiyenko: Physical and Theoretical Chemistry Laboratory, University of Oxford
Carla Schmidt: Physical and Theoretical Chemistry Laboratory, University of Oxford
Martin D. Jennings: Faculty of Life Sciences, Michael Smith Building, University of Manchester
Dijana Matak-Vinkovic: University of Cambridge
Graham D. Pavitt: Faculty of Life Sciences, Michael Smith Building, University of Manchester
Carol V. Robinson: Physical and Theoretical Chemistry Laboratory, University of Oxford

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract eIF2B facilitates and controls protein synthesis in eukaryotes by mediating guanine nucleotide exchange on its partner eIF2. We combined mass spectrometry (MS) with chemical cross-linking, surface accessibility measurements and homology modelling to define subunit stoichiometry and interactions within eIF2B and eIF2. Although it is generally accepted that eIF2B is a pentamer of five non-identical subunits (α–ε), here we show that eIF2B is a decamer. MS and cross-linking of eIF2B complexes allows us to propose a model for the subunit arrangements within eIF2B where the subunit assembly occurs through catalytic γ- and ε-subunits, with regulatory subunits arranged in asymmetric trimers associated with the core. Cross-links between eIF2 and eIF2B allow modelling of interactions that contribute to nucleotide exchange and its control by eIF2 phosphorylation. Finally, we identify that GTP binds to eIF2Bγ, prompting us to propose a multi-step mechanism for nucleotide exchange.

Date: 2014
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DOI: 10.1038/ncomms4902

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