Specific thiol compounds complement deficiency in c‐type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane‐bound disulphide isomerase‐like protein

FEBS Letters

Ferguson, Stuart J.¹  Sambongi, Yoshihiro¹ 

[1] Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

关键词: Bacterial c-type cytochrome biogenesis;    Protein disulphide isomerase;    l-Cysteine;    AP;    alkaline phosphatase;    PCR;    polymerase chain reaction;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)01053-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Escherichia coli JCB606 carries a mutation in the dipZ gene, known to code for a disulphide isomerase-like protein, with the consequence that holo forms of neither exogenous nor endogenous c-type cytochromes are synthesised. This failure has been overcome by adding compounds containing thiol groups to the growth medium. Only l-Cysteine and 2-mercaptoethane sulphonic acid were effective, suggesting a (stereo)specific binding site that could be occupied by these compounds in the absence of the catalytic domain of DipZ.

【 授权许可】

Unknown