Overproduction and purification of McrC protein from Escherichia coli K-12.
The McrC protein, encoded by one of the two genes involved in the McrB restriction system, was produced in Escherichia coli cells by using a T7 expression system. Following sequential DEAE-Sepharose and hydroxylapatite column chromatography, the protein was purified to apparent homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence of the purified McrC protein agreed exactly with the one deduced from the DNA sequence by Ross et al. (J. Bacteriol. 171:1974-1981, 1989).
Zheng
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Department of Microbiology, Louisiana State University, Baton Rouge 70803.
Braymer
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HD
D001345:Autoradiography; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D004262:DNA Restriction Enzymes; D015257:DNA-Cytosine Methylases / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D016366:Open Reading Frames; D010957:Plasmids; D015183:Restriction Mapping
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C069326:mcrC protein, E coli; C059683:DNA modification methylase McrB; D015257:DNA-Cytosine Methylases; D004262:DNA Restriction Enzymes