期刊
NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms4902
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资金
- Wellcome Trust [088150/B/09/Z]
- BBSRC [BB/H010599/1]
- BBSRC [BB/L000652/1, BB/F013272/1, BB/H010599/1] Funding Source: UKRI
- MRC [MC_U105184332] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H010599/1, BB/F013272/1, BB/L000652/1] Funding Source: researchfish
- Medical Research Council [MC_U105184332] Funding Source: researchfish
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 (alpha-epsilon), 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 gamma- and epsilon-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 eIF2B gamma, prompting us to propose a multi-step mechanism for nucleotide exchange.
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