A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

被引：146

作者：

Sevier, CS ^{[1
]}

Cuozzo, JW ^{[1
]}

Vala, A ^{[1
]}

Åslund, F ^{[1
]}

Kaiser, CA ^{[1
]}

机构：

[1] MIT, Dept Biol, Cambridge, MA 02139 USA

来源：

NATURE CELL BIOLOGY | 2001年 / 3卷 / 10期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/ncb1001-874

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Ero1 and Pdi1 are essential elements of the pathway for the formation of disulphide bonds within the endoplasmic reticulum (ER). By screening for alternative oxidation pathways in Saccharomyces cerevisiae, we identified EM as a gene that when overexpressed can restore viability and disulphide bond formation to an ero1-1 mutant strain. EM encodes a luminal ER protein of relative molecular mass 22,000. Purified recombinant Erv2p is a flavoenzyme that can catalyse O-2-dependent formation of disulphide bonds. Erv2p transfers oxidizing equivalents to Pdi1p by a dithiol-disulphide exchange reaction, indicating that the Erv2p-dependent pathway for disulphide bond formation closely parallels that of the previously identified Ero1p-dependent pathway.

引用

页码：874 / 882

页数：9

共 38 条

[1] ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum [J].