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

Author

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  • Yuliya Gordiyenko

    (Physical and Theoretical Chemistry Laboratory, University of Oxford
    MRC Laboratory of Molecular Biology, University of Cambridge)

  • 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)

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.

Suggested Citation

  • Yuliya Gordiyenko & Carla Schmidt & Martin D. Jennings & Dijana Matak-Vinkovic & Graham D. Pavitt & Carol V. Robinson, 2014. "eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core," Nature Communications, Nature, vol. 5(1), pages 1-12, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4902
    DOI: 10.1038/ncomms4902
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