Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c‐type cytochrome except in the presence of disulphide compounds
Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c‐type cytochrome except in the presence of disulphide compounds
复制标题
缺乏二硫键氧化还原酶 DsbA 和 DsbB 的大肠杆菌突变体除非存在二硫键化合物，否则无法合成外源单血红素 C 型细胞色素
DOI：
10.1016/s0014-5793(96)01256-2
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发表时间：
1996
期刊：
影响因子：
3.5
通讯作者：
S. Ferguson
中科院分区：
文献类型：
--
作者：
Y. Sambongi;S. Ferguson
通过突变参与周质二硫键形成的两种蛋白质DsbA和DsbB，导致厌氧生长的大肠杆菌不能合成其内源性c型细胞色素亚硝酸还原酶或来自副球菌的外源性细胞色素c550的全形式。通过在生长培养基中加入含有二硫键的化合物，谷胱甘肽的氧化形式。结果表明，血红素的附着到CXXCH基序的周质C-型细胞色素可能precancelled通过形成一个或多个内或分子间二硫键，涉及该基序的半胱氨酸残基。
Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown Escherichia coli to synthesise the holo forms of either its endogenous c-type cytochrome nitrite reductase or exogenous cytochrome c550from Paracoccus denitrificans. The synthesis of both cytochromes can be restored to the mutants by inclusion in the growth media of compounds containing disulphide bonds, e.g., the oxidised form of glutathione. The results suggest that the attachment of haem to the CXXCH motif of a periplasmic c-type cytochrome may be preceeded by the formation of one or more intra- or intermolecular disulphide bonds involving the cysteine residues of this motif.