Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
Copyright policy )Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
The endoplasmic reticulum (ER) supports disulfide bond formation by a poorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1. In yeast, Ero1p-mediated oxidative folding was shown to depend on cellular flavin adenine dinucleotide (FAD) levels but not on ubiquinone or heme, and Ero1p was shown to be a FAD-binding protein. We reconstituted efficient oxidative folding in vitro using FAD, PDI, and Ero1p. Disulfide formation proceeded by direct delivery of oxidizing equivalents from Ero1p to folding substrates via PDI. This kinetic shuttling of oxidizing equivalents could allow the ER to support rapid disulfide formation while maintaining the ability to reduce and rearrange incorrect disulfide bonds.
- Howard Hughes Medical Institute United States
- University of California, San Francisco United States
Protein Folding, Binding Sites, Saccharomyces cerevisiae Proteins, Chemical Phenomena, Chemistry, Physical, Protein Disulfide-Isomerases, Cathepsin A, Carboxypeptidases, Ribonuclease, Pancreatic, Saccharomyces cerevisiae, Endoplasmic Reticulum, Glutathione, Microsomes, Mutation, Flavin-Adenine Dinucleotide, Oxidoreductases Acting on Sulfur Group Donors, Disulfides, Oxidation-Reduction, Glycoproteins
Protein Folding, Binding Sites, Saccharomyces cerevisiae Proteins, Chemical Phenomena, Chemistry, Physical, Protein Disulfide-Isomerases, Cathepsin A, Carboxypeptidases, Ribonuclease, Pancreatic, Saccharomyces cerevisiae, Endoplasmic Reticulum, Glutathione, Microsomes, Mutation, Flavin-Adenine Dinucleotide, Oxidoreductases Acting on Sulfur Group Donors, Disulfides, Oxidation-Reduction, Glycoproteins
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