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

  1. Lookup NU author(s)
  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
Year1985
Volume260
Issue2
Pages1224-1229
ISSN (print)0021-9258
ISSN (electronic)1083-351X
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
URLhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3155726
Notes0021-9258 Journal Article
Actions    Link to this publication