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A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases

Author

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  • Andrew F. Voter

    (University of Wisconsin School of Medicine and Public Health)

  • Yupeng Qiu

    (Johns Hopkins University)

  • Ramreddy Tippana

    (Johns Hopkins University)

  • Sua Myong

    (Johns Hopkins University)

  • James L. Keck

    (University of Wisconsin School of Medicine and Public Health)

Abstract

Homeostatic regulation of G-quadruplexes (G4s), four-stranded structures that can form in guanine-rich nucleic acids, requires G4 unwinding helicases. The mechanisms that mediate G4 unwinding remain unknown. We report the structure of a bacterial RecQ DNA helicase bound to resolved G4 DNA. Unexpectedly, a guanine base from the unwound G4 is sequestered within a guanine-specific binding pocket. Disruption of the pocket in RecQ blocks G4 unwinding, but not G4 binding or duplex DNA unwinding, indicating its essential role in structure-specific G4 resolution. A novel guanine-flipping and sequestration model that may be applicable to other G4-resolving helicases emerges from these studies.

Suggested Citation

  • Andrew F. Voter & Yupeng Qiu & Ramreddy Tippana & Sua Myong & James L. Keck, 2018. "A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06751-8
    DOI: 10.1038/s41467-018-06751-8
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    Cited by:

    1. Zebin Hong & Alicia K. Byrd & Jun Gao & Poulomi Das & Vanessa Qianmin Tan & Emory G. Malone & Bertha Osei & John C. Marecki & Reine U. Protacio & Wayne P. Wahls & Kevin D. Raney & Haiwei Song, 2024. "Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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