The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation.
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Wang L, Zhu L, Wang CC
The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation.
Biochem J. 2011 Feb 15;434(1):113-21. doi: 10.1042/BJ20101357.
- PubMed ID
- 21091435 [ View in PubMed]
- Abstract
In eukaryotes, disulfide bonds are formed in the endoplasmic reticulum, facilitated by the Ero1 (endoplasmic reticulum oxidoreductin 1) oxidase/PDI (protein disulfide-isomerase) system. Mammals have two ERO1 genes, encoding Ero1alpha and Ero1beta proteins. Ero1beta is constitutively expressed in professional secretory tissues and induced during the unfolded protein response. In the present work, we show that recombinant human Ero1beta is twice as active as Ero1alpha in enzymatic assays. Ero1beta oxidizes PDI more efficiently than other PDI family members and drives oxidative protein folding preferentially via the active site in the a domain of PDI. Our results reveal that Ero1beta oxidase activity is regulated by long-range disulfide bonds and that Cys130 plays a critical role in feedback regulation. Compared with Ero1alpha, however, Ero1beta is loosely regulated, consistent with its role as a more active oxidase when massive oxidative power is required.