A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases
Andrew F. Voter,
Yupeng Qiu,
Ramreddy Tippana,
Sua Myong and
James L. Keck ()
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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
Nature Communications, 2018, vol. 9, issue 1, 1-8
Abstract:
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.
Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06751-8
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DOI: 10.1038/s41467-018-06751-8
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