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

Lookup NU author(s): Professor Craig Robson, Professor Peter Emmerson

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Abstract

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.


Publication metadata

Author(s): Hickson ID, Robson CN, Atkinson KE, Hutton L, Emmerson PT

Publication type: Article

Journal: Journal of Biological Chemistry

Year: 1985

Volume: 260

Issue: 2

Pages: 1224-1229

Print publication date: 25/01/1985

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3155726

Notes: 0021-9258 Journal Article


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