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RHAU helicase specifically resolves thermodynamically stable four-stranded G-quadruplex(G4)structures that are implicated in a wide array of biological processes.Importantly,RHAU has been suggested to be a major source of G4 resolving activity in cells.Through direct probing the G4 stability at single-molecule level,we show that binding of RHAU stabilizes G4 in the absence of nucleotide,while it destabilizes G4 when coupled to ATP hydrolysis.We also show that the unfolding kinetics of a G4 structure can be modulated by different ATPase states of RHAU.These findings provide important insights into the ATP-dependent RHAU-mediated G4 destabilization mechanism.