The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding

Paul E Boehmer, Peter T. Emmerson

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

The RecB subunit of the Escherichia coli RecBCD enzyme has previously been reported to possess DNA-dependent ATPase activity (Hickson, I. D., Robson, C. N., Atkinson, K. E., Hutton, L., and Emmerson, P. T. (1985) J. Biol. Chem. 260, 1224-1229). Here we demonstrate that a specific interaction between RecB protein and ATP can also be shown by photoaffinity labeling with the ATP analogue 8-azido-ATP. Furthermore, the capacity of the RecB protein to support ATP hydrolysis varies with the structure and length of the DNA cofactor. Single-stranded linear and circular DNA are markedly better in promoting ATP hydrolysis than duplex DNA. The purified RecB protein can function as a DNA helicase, displacing oligonucleotides annealed to viral M13 DNA in an ATP-dependent and orientation-specific manner.

Original languageEnglish (US)
Pages (from-to)4981-4987
Number of pages7
JournalJournal of Biological Chemistry
Volume267
Issue number7
StatePublished - Mar 5 1992
Externally publishedYes

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Exodeoxyribonuclease V
Escherichia coli
Hydrolysis
Adenosine Triphosphate
DNA
DNA Helicases
Circular DNA
Proteins
Single-Stranded DNA
Viral DNA
Oligonucleotides
Labeling
Adenosine Triphosphatases

ASJC Scopus subject areas

  • Biochemistry

Cite this

The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding. / Boehmer, Paul E; Emmerson, Peter T.

In: Journal of Biological Chemistry, Vol. 267, No. 7, 05.03.1992, p. 4981-4987.

Research output: Contribution to journalArticle

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