Multiple RPAs make WRN syndrome protein a superhelicase

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...

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Published inNucleic acids research Vol. 46; no. 9; pp. 4689 - 4698
Main Authors Lee, Mina, Shin, Soochul, Uhm, Heesoo, Hong, Heesun, Kirk, Jaewon, Hyun, Kwangbeom, Kulikowicz, Tomasz, Kim, Jaehoon, Ahn, Byungchan, Bohr, Vilhelm A, Hohng, Sungchul
Format Journal Article
LanguageEnglish
Published England Oxford University Press 18.05.2018
Subjects
Fluorescence Resonance Energy Transfer
Humans
Nucleic Acid Enzymes
Replication Protein A - metabolism
Werner Syndrome Helicase - metabolism
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Summary: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.
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The authors wish it to be known that, in their opinion, the first three authors should be regarded as Joint First Authors.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gky272