Oxidative protein folding is driven by the electron transport system

被引：321

作者：

Bader, M

Muse, W

Ballou, DP

Gassner, C

Bardwell, JCA

机构：

[1] Univ Michigan, Dept Biol, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

CELL | 1999年 / 98卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0092-8674(00)81016-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Disulfide bond formation is catalyzed in vivo by DsbA and DsbB. Here we reconstitute this oxidative folding system using purified components. We have found the sources of oxidative power for protein folding and show how disulfide bond formation is linked to cellular metabolism. We find that disulfide bond formation and the electron transport chain are directly coupled. DsbB uses quinones as electron accepters, allowing various choices for electron transport to support disulfide bond formation. Electrons flow via cytochrome bo oxidase to oxygen under aerobic conditions or via cytochrome bd oxidase under partially anaerobic conditions. Under truly anaerobic conditions, menaquinone shuttles electrons to alternate final electron accepters such as fumarate. This flexibility reflects the vital nature of the disulfide catalytic system.

引用

页码：217 / 227

页数：11

共 34 条

[1] A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins [J].