ATPase-dependent duplex nucleic acid unwinding by SARS-CoV-2 nsP13 relies on facile binding and translocation along single-stranded nucleic acid.

ABSTRACT: Nonstructural protein 13 (nsP13) of severe acute respiratory syndrome coronary virus (SARS-CoV-2) is a superfamily one helicase, which is essential for viral RNA replication. This protein can unwind dsRNA and DNA with a 5' single-stranded tail in the 5'-3' direction. Previous studies have demonstrated that nsP13 efficiently unwinds double-stranded nucleic acids with a single-stranded tail through a cooperative translocation fueled by ATP hydrolysis. However, the mechanism underlying the aforementioned unwinding remains unclear. In this study, we hypothesized that the differences in unwinding efficiency among duplex nucleic acids are driven by the ATP hydrolysis-induced changes in the binding affinity of nsP13 to a single-stranded tail. When nsP13 unwinds dsDNA with a 5' single-stranded tai

SUBMITTER: Park J 

PROVIDER: S-EPMC12274814 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature