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Pré-Publication, Document De Travail Année : 2020

DHX36-mediated G-quadruplex unfolding is ATP-independent?

Hai-Lei Guo
  • Fonction : Auteur
Wei-Fei Chen
  • Fonction : Auteur
Na-Nv Liu
  • Fonction : Auteur
Ze-Yu Song
  • Fonction : Auteur
Yan-Xue Dai
  • Fonction : Auteur
Xi-Miao Hou
  • Fonction : Auteur
Shuo-Xing Dou
  • Fonction : Auteur

Résumé

Chen et al. solved the crystal structure of bovine DHX36 bound to a DNA with a G-quadruplex (G4) and a single-stranded DNA segment. They believed that the mechanism they proposed may represent a general model for describing how a G4-unfolding helicase recognizes and unfolds G4 DNA. Their conclusion is interesting, however, we noticed that their linear DNA substrate (DNAMyc) that harbors a Myc-promoter-derived G4-forming sequence was directly used without pre-folding. This raises the question whether the structure they obtained really reflects DHX36-mediated G4 recognition and unfolding, or just only represents a DHX36-binding-induced quasi-folded G4 structure. By a combination of polymerase extension, DMS footprinting, stopped-flow, and smFRET assays, we obtained clear evidences that do not support their ATP-independent one-base translocation structural model. We further revealed that the oscillation of FRET signal they observed should correspond to a repetitive G4 binding, but not unfolding, by DHX36.
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Dates et versions

hal-03013152 , version 1 (18-11-2020)

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Hai-Lei Guo, Wei-Fei Chen, Stéphane Réty, Na-Nv Liu, Ze-Yu Song, et al.. DHX36-mediated G-quadruplex unfolding is ATP-independent?. 2020. ⟨hal-03013152⟩
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