A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases
Journal Article
·
· Nature Communications
- Univ. of Wisconsin School of Medicine and Public Health, Madison, WI (United States); DOE/OSTI
- Johns Hopkins Univ., Baltimore, MD (United States)
- Univ. of Wisconsin School of Medicine and Public Health, Madison, WI (United States)
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.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- NIH; USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1478097
- Journal Information:
- Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 9; ISSN 2041-1723
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
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