PMID:6090429
| Citation |
Heincz, MC, Bornstein, SM and McFall, E (1984) Purification and characterization of D-serine deaminase activator protein. J. Bacteriol. 160:42-9 |
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| Abstract |
We purified the dsdC gene product, the specific activator of dsdA (D-serine deaminase) gene expression, to about 25% homogeneity from a strain in which its expression was amplified 100-fold. The purification involved, successively: DNase and high-salt treatment of cell extracts, DNA-cellulose chromatography, and Dyematrex (Amicon Corp.) column chromatography. We identified the protein as a discrete spot on two-dimensional O'Farrell gels after the DNA-cellulose step and quantitated it by densitometry. The active form was found to be a dimer. We estimated that there were eight activator dimers per wild-type cell. The activator is a slightly basic protein, with an experimental Km for its ligand D-serine of about 7 X 10(-6)M. The low concentration of the activator in wild-type cells and its autorepression may explain the previously observed partial dominance of dsdC+ in dsdCc/dsdC+ merodiploids. |
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| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; DNA Restriction Enzymes; DNA, Recombinant/metabolism; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Escherichia coli/enzymology; Escherichia coli/genetics; Genotype; Kinetics; L-Serine Dehydratase/genetics; L-Serine Dehydratase/metabolism; Plasmids; Species Specificity |
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