Reconstitution of RecBC DNase activity from purified Escherichia coli RecB and RecC proteins

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  2. Professor Craig Robson
  3. Professor Peter Emmerson
Author(s)Hickson ID, Robson CN, Atkinson KE, Hutton L, Emmerson PT
Publication type Article
JournalJournal of Biological Chemistry
ISSN (print)0021-9258
ISSN (electronic)1083-351X
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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.
Notes0021-9258 Journal Article
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