期刊
CELL
卷 151, 期 4, 页码 794-806出版社
CELL PRESS
DOI: 10.1016/j.cell.2012.09.036
关键词
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资金
- NIH [HL066030, HL061228, CA097061, CA161061, GM085081]
- HHMI
- Arnold and Mabel Beckman Foundation
- Spanish Ministry of Education
- Spanish Ministry of Science and Innovation [BIO2009-09562, CSD2009-00088]
- FEDER
- Fundacion Ibercaja
- Training Program in Molecular Biophysics [T32GM008281]
- Fulbright scholarship
PDI catalyzes the oxidative folding of disulfide-containing proteins. However, the sequence of reactions leading to a natively folded and oxidized protein remains unknown. Here we demonstrate a technique that enables independent measurements of disulfide formation and protein folding. We find that non-native disulfides are formed early in the folding pathway and can trigger misfolding. In contrast, a PDI domain favors native disulfides by catalyzing oxidation at a late stage of folding. We propose a model for cotranslational oxidative folding wherein PDI acts as a placeholder that is relieved by the pairing of cysteines caused by substrate folding. This general mechanism can explain how PDI catalyzes oxidative folding in a variety of structurally unrelated substrates.
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