Selected article for: "ATP hydrolysis activity and unwinding activity"
Author: Lee, Na-Ra; Kwon, Hyun-Mi; Park, Kkothanahreum; Oh, Sangtaek; Jeong, Yong-Joo; Kim, Dong-Eun
Title: Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13
  • Document date: 2010_7_29
    • ID: 1k99yv4i_13
    Snippet: SCV helicase nsP13 has been shown to have dsDNA unwinding activity and was shown to belong to the family of SF1 helicases (28) . Like many SF1 helicases, the SCV helicase requires an exposed ss DNA or RNA for binding to the nucleic acid complex and the helicase translocates along the nucleic acids by hydrolyzing ATP. We have previously shown that ss DNA or RNA stimulates the ATP hydrolysis activity, but dsDNA does not (25) . Although the crystal .....
    Document: SCV helicase nsP13 has been shown to have dsDNA unwinding activity and was shown to belong to the family of SF1 helicases (28) . Like many SF1 helicases, the SCV helicase requires an exposed ss DNA or RNA for binding to the nucleic acid complex and the helicase translocates along the nucleic acids by hydrolyzing ATP. We have previously shown that ss DNA or RNA stimulates the ATP hydrolysis activity, but dsDNA does not (25) . Although the crystal structures of a few typical SF1 helicases complexed with DNA were revealed (29,30), e.g. Rep and PcrA, only a computational 3D model has been proposed for the SCV helicase nsP13 (20) . Therefore, details about the nucleic acid unwinding mechanism of SCV helicase nsP13 have to be deduced from biochemical studies only. Hence, we investigated how the mechanistic efficiency of dsDNA unwinding by nsP13 is affected by the structural features of the dsDNAs, such as duplex length, ssDNA tail length and artificial ss gap between the two DNA duplexes.

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