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Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks

Author

Listed:
  • Martin R. Singleton

    (The London Research Institute, Blanche Lane, South Mimms, Potters Bar)

  • Mark S. Dillingham

    (National Institute for Medical Research, The Ridgeway)

  • Martin Gaudier

    (The London Research Institute, Blanche Lane, South Mimms, Potters Bar)

  • Stephen C. Kowalczykowski

    (University of California at Davis)

  • Dale B. Wigley

    (The London Research Institute, Blanche Lane, South Mimms, Potters Bar)

Abstract

RecBCD is a multi-functional enzyme complex that processes DNA ends resulting from a double-strand break. RecBCD is a bipolar helicase that splits the duplex into its component strands and digests them until encountering a recombinational hotspot (Chi site). The nuclease activity is then attenuated and RecBCD loads RecA onto the 3′ tail of the DNA. Here we present the crystal structure of RecBCD bound to a DNA substrate. In this initiation complex, the DNA duplex has been split across the RecC subunit to create a fork with the separated strands each heading towards different helicase motor subunits. The strands pass along tunnels within the complex, both emerging adjacent to the nuclease domain of RecB. Passage of the 3′ tail through one of these tunnels provides a mechanism for the recognition of a Chi sequence by RecC within the context of double-stranded DNA. Gating of this tunnel suggests how nuclease activity might be regulated.

Suggested Citation

  • Martin R. Singleton & Mark S. Dillingham & Martin Gaudier & Stephen C. Kowalczykowski & Dale B. Wigley, 2004. "Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks," Nature, Nature, vol. 432(7014), pages 187-193, November.
    • Handle: RePEc:nat:nature:v:432:y:2004:i:7014:d:10.1038_nature02988
    DOI: 10.1038/nature02988
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    Cited by:

    1. Aviv Meir & Vivek B. Raina & Carly E. Rivera & Léa Marie & Lorraine S. Symington & Eric C. Greene, 2023. "The separation pin distinguishes the pro– and anti–recombinogenic functions of Saccharomyces cerevisiae Srs2," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Kai Zhou & Chun-Xu Xue & Tingting Xu & Ping Shen & Sha Wei & Kelly L. Wyres & Margaret M. C. Lam & Jinquan Liu & Haoyun Lin & Yunbo Chen & Kathryn E. Holt & Yonghong Xiao, 2023. "A point mutation in recC associated with subclonal replacement of carbapenem-resistant Klebsiella pneumoniae ST11 in China," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. 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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