Abstract RPA is known to stimulate the helicase activity of Werner syndrome protein (WRN), but the exact stimulation mechanism is not understood. We use single-molecule FRET and magnetic tweezers to investigate the helicase activity of WRN and its stimulation by RPA. We show that WRN alone is a weak helicase which repetitively unwind just a few tens of base pairs, but that binding of multiple RPAs to the enzyme converts WRN into a superhelicase that unidirectionally unwinds double-stranded DNA more than 1 kb. Our study provides a good case in which the activity and biological functions of the enzyme may be fundamentally altered by the binding of cofactors.
Multiple RPAs make WRN syndrome protein a superhelicase
Mina Lee,Soochul Shin,Heesoo Uhm,Heesun Hong,Jaewon Kirk,K. Hyun,Tomasz Kulikowicz,Jaehoon Kim,B. Ahn,V. Bohr,S. Hohng
Published 2018 in Nucleic Acids Research
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- Publication year
2018
- Venue
Nucleic Acids Research
- Publication date
2018-04-14
- Fields of study
Biology, Medicine
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Semantic Scholar, PubMed
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