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RecBCD enzyme is a bipolar DNA helicase

Author

Listed:
  • Mark S. Dillingham

    (University of California
    National Institute for Medical Research, The Ridgeway)

  • Maria Spies

    (University of California)

  • Stephen C. Kowalczykowski

    (University of California)

Abstract

Escherichia coli RecBCD is a heterotrimeric helicase/nuclease that catalyses a complex reaction in which double-strand breaks in DNA are processed for repair by homologous recombination1. For some time it has been clear that the RecB subunit possesses a 3′ → 5′ DNA helicase activity2,3,4, which was thought to drive DNA translocation and unwinding in the RecBCD holoenzyme. Here we show that purified RecD protein is also a DNA helicase, but one that possesses a 5′ → 3′ polarity. We also show that the RecB and RecD helicases are both active in intact RecBCD, because the enzyme remains capable of processive DNA unwinding when either of these subunits is inactivated by mutation. These findings point to a bipolar translocation model for RecBCD in which the two DNA helicases are complementary, travelling with opposite polarities, but in the same direction, on each strand of the antiparallel DNA duplex. This bipolar motor organization helps to explain various biochemical properties of RecBCD, notably its exceptionally high speed and processivity, and offers a mechanistic insight into aspects of RecBCD function.

Suggested Citation

  • Mark S. Dillingham & Maria Spies & Stephen C. Kowalczykowski, 2003. "RecBCD enzyme is a bipolar DNA helicase," Nature, Nature, vol. 423(6942), pages 893-897, June.
    • Handle: RePEc:nat:nature:v:423:y:2003:i:6942:d:10.1038_nature01673
    DOI: 10.1038/nature01673
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    Cited by:

    1. Rani Zananiri & Sivasubramanyan Mangapuram Venkata & Vera Gaydar & Dan Yahalom & Omri Malik & Sergei Rudnizky & Oded Kleifeld & Ariel Kaplan & Arnon Henn, 2022. "Auxiliary ATP binding sites support DNA unwinding by RecBCD," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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