The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo

被引:87
作者
Fabianek, RA [1 ]
Hennecke, H [1 ]
Thöny-Meyer, L [1 ]
机构
[1] Swiss Fed Inst Technol, Inst Mikrobiol, CH-8092 Zurich, Switzerland
关键词
D O I
10.1128/JB.180.7.1947-1950.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A new member of the family of periplasmic protein thiol:disulfide oxidareductases, CcmG (also called DsbE), was characterized with regard to its role in cytochrome c maturation in Escherichia coli. The CcmG protein was shown to be membrane bound, facing the periplasm with its C-terminal, hydrophilic domain. A chromosomal, nonpolar in-frame deletion in ccmG resulted in the complete absence of all c-type cytochromes. Replacement of either one or both of the two cysteine residues of the predicted active site in CcmG (WCPTC) led to low but detectable levels of Bradyrhizobium japonicum holocytochrome c(550) expressed in E. coli. This defect, but not that of the ccmG null mutant, could be complemented by adding low-molecular-weight thiol compounds to growing cells, which is in agreement with a reducing function for CcmG.
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收藏
页码:1947 / 1950
页数:4
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