Multiple RPAs make WRN syndrome protein a superhelicase

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...

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Detalles Bibliográficos
Autores principales: Lee, Mina, Shin, Soochul, Uhm, Heesoo, Hong, Heesun, Kirk, Jaewon, Hyun, Kwangbeom, Kulikowicz, Tomasz, Kim, Jaehoon, Ahn, Byungchan, Bohr, Vilhelm A, Hohng, Sungchul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Nucleic Acid Enzymes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5961295/
https://www.ncbi.nlm.nih.gov/pubmed/29668972
http://dx.doi.org/10.1093/nar/gky272
Descripción
Sumario: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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