An engineered pathway for the formation of protein disulfide bonds
An engineered pathway for the formation of protein disulfide bonds
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DOI：
10.1126/science.1092612
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发表时间：
2004-02-20
期刊：
影响因子：
56.9
通讯作者：
Collet, JF
中科院分区：
文献类型：
--
作者：
Masip, L;Pan, JL;Collet, JF
We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is a monomeric disulfide reductase, into a [2Fe-2S] bridged dimer capable of catalyzing O-2-dependent sulfhydryl oxidation in vitro. Expression of the mutant protein in Escherichia coli with oxidizing cytoplasm and secretion via the Tat pathway restored disulfide bond formation in strains that lacked the complete periplasmic oxidative machinery (DsbA and DsbB). The evolution of [2Fe-2S] thioredoxin illustrates how mutations within an existing scaffold can add a cofactor and markedly change protein function.
