Faculty Opinions recommendation of A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases.
Year: 2019
Type: peer-review
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.
Author: Brandt Eichman
Institution: Vanderbilt University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: G102163711, G107546177, G1313983767, G1505794299, G1664757510, G1947107004, G2101401529, G2287611682, G262962599, G2887060908, G2896567508, G3075337988, G3329398301, G340565428, G416541740, G4773269573, G498139845, G5106849484, G5520316217, G5607048534, G5906309288, G6101244626, G6848031779, G6918803902, Identification of chemosensitizing agents that block DNA repair by the Fanconi Anemia/Bloom Dissolvasome complex, G7147508703, G7368700025, Integrated Training For Physician-Scientists, G8764064047, Structure and Function of the Bacterial Primosome, G969889393, G993149817
OpenAlex ID: W4235219830