Science. 2000 Nov 24;290(5496):1571-4.

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.

Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS.

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Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.

Abstract

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.

Comment in

Dev Cell. 2002 Dec;3(6):758-60.

PMID:: 11090354; [PubMed - indexed for MEDLINE]

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Biochemical basis of oxidative protein folding in the endoplasmic reticulum.

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