Lookup NU author(s): Professor Craig Robson,
Professor Peter Emmerson
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The Escherichia coli RecB protein, normally synthesized in low amounts, has been amplified by linkage of the recB gene to the phage lambda leftward promoter in an expression plasmid. From strains harboring this plasmid, RecB protein has been purified to homogeneity by a simple procedure which includes affinity chromatography on a column of RecC protein bound to agarose. The purified RecB protein has DNA-dependent ATPase activity but no exonuclease activity. RecC protein alone has neither ATPase nor exonuclease activity. However, when combined together, the RecB and RecC proteins show the ATP-dependent double-stranded exonuclease properties characteristic of the RecBC DNase.
Author(s): Hickson ID, Robson CN, Atkinson KE, Hutton L, Emmerson PT
Publication type: Article
Journal: Journal of Biological Chemistry
Print publication date: 25/01/1985
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X