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Biochemical and Genetic Studies of Recombination Proficiency in <i>Escherichia coli</i> , I. Enzymatic Activity Associated with <i>recB</i> <sup>+</sup> and <i>recC</i> <sup>+</sup> Genes

Proceedings of the National Academy of SciencesPublished 1 April 1970Open access
Stephen D. Barbour, Alvin J. Clark
Citations197
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TL;DR

An adenosine triphosphate-dependent deoxyribonuclease activity has been detected in lysates of recB(+)recC(+) strains, and mutations in recB or recC lead to loss of this activity, suggesting that these two genes determine the nucleaseActivity.

Abstract

An adenosine triphosphate-dependent deoxyribonuclease activity has been detected in lysates of recB(+)recC(+) strains. Mutations in recB or recC lead to loss of this activity, suggesting that these two genes determine the nuclease activity. The over-all reaction in crude lysates digests native DNA to nucleoside monophosphates. Complementation between recB21 and recC22 in vivo leads to normal levels of ATP-dependent nuclease activity. No complementation in vitro has been detected. Mutations in a third recombination gene (recA) do not alter significantly the wild-type levels of this nuclease activity.

Keywords

Biochemistry, Genetics and Molecular Biology