Journal article
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 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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 2.9MB, Terms of use)
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- Publisher copy:
- 10.1093/nar/gky272
Authors
- Publisher:
- Oxford University Press
- Journal:
- Nucleic Acids Research More from this journal
- Volume:
- 46
- Issue:
- 9
- Pages:
- 4689-4698
- Publication date:
- 2018-04-14
- Acceptance date:
- 2018-04-11
- DOI:
- EISSN:
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1362-4962
- ISSN:
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0305-1048
- Pmid:
-
29668972
- Language:
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English
- Keywords:
- Pubs id:
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pubs:979103
- UUID:
-
uuid:57b00a09-a2d9-470b-a1c2-9d1956f915ad
- Local pid:
-
pubs:979103
- Source identifiers:
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979103
- Deposit date:
-
2019-03-11
Terms of use
- Copyright holder:
- Lee et al
- Copyright date:
- 2018
- Notes:
- © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License.
- Licence:
- CC Attribution (CC BY)
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