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

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  • Wojciech W. Krajewski

    (Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK
    Present address: CRT Discovery Laboratories, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, 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)

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.

Suggested Citation

  • Wojciech W. Krajewski & Xin Fu & Martin Wilkinson & Nora B. Cronin & Mark S. Dillingham & Dale B. Wigley, 2014. "Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites," Nature, Nature, vol. 508(7496), pages 416-419, April.
    • Handle: RePEc:nat:nature:v:508:y:2014:i:7496:d:10.1038_nature13037
    DOI: 10.1038/nature13037
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