Multiple RPAs make WRN syndrome protein a superhelicase

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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.
Publisher
OXFORD UNIV PRESS
Issue Date
2018-05
Language
English
Article Type
Article
Citation

NUCLEIC ACIDS RESEARCH, v.46, no.9, pp.4689 - 4698

ISSN
0305-1048
DOI
10.1093/nar/gky272
URI
http://hdl.handle.net/10203/242541
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
2018 Lee & Hohng_NAR.pdf(2.95 MB)Download
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