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Chen et al. solved the crystal structure of bovine DHX36 bound to a DNA witha G-quadruplex (G4) and a single-stranded DNA segment. They believed that themechanism they proposed may represent a general model for describing how aG4-unfolding helicase recognizes and unfolds G4 DNA. Their conclusion isinteresting, however, we noticed that their linear DNA substrate (DNAMyc) thatharbors a Myc-promoter-derived G4-forming sequence was directly used withoutpre-folding. This raises the question whether the structure they obtainedreally reflects DHX36-mediated G4 recognition and unfolding, or just onlyrepresents a DHX36-binding-induced quasi-folded G4 structure. By a combinationof polymerase extension, DMS footprinting, stopped-flow, and smFRET assays, weobtained clear evidences that do not support their ATP-independent one-basetranslocation structural model. We further revealed that the oscillation ofFRET signal they observed should correspond to a repetitive G4 binding, but notunfolding, by DHX36.

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