PMID:7957865
| Citation |
Sambongi, Y and Ferguson, SJ (1994) 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 Lett. 353:235-8 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Alkaline Phosphatase/genetics; Alkaline Phosphatase/metabolism; Base Sequence; Cell Fractionation; Culture Media; Cytochrome c Group/biosynthesis; Cytochrome c Group/genetics; Disulfides/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Isomerases/genetics; Isomerases/metabolism; Molecular Sequence Data; Mutation/physiology; Protein Disulfide-Isomerases; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/metabolism; Sulfhydryl Compounds/metabolism |
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