Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites

Wojciech W. Krajewski, Xin Fu, Martin Wilkinson, Nora B. Cronin, Mark S. Dillingham and Dale B. Wigley ()
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Wojciech W. Krajewski: Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK
Xin Fu: Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK
Martin Wilkinson: Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK
Nora B. Cronin: Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK
Mark S. Dillingham: School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK
Dale B. Wigley: Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK

Nature, 2014, vol. 508, issue 7496, 416-419

Abstract: A dual-function helicase–nuclease, typified by RecBCD in Escherichia coli, acts on free DNA ends during bacterial double-stranded break repair until it reaches a χ sequence at which it pauses before continuing with modified enzymatic properties; here several crystal structures of the related AddAB enzyme from Bacillus subtilis bound to χ-containing DNA are presented, offering insight into χ recognition and its effect on DNA translocation.

Date: 2014
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DOI: 10.1038/nature13037

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