Macmaster, R., Sedelnikova, S., Baker, P. J. orcid.org/0000-0003-1995-5643 et al. (3 more authors) (2006) RusA Holliday junction resolvase: DNA complex structure - insights into selectivity and specificity. Nucleic Acids Research, 34 (19). pp. 5577-5584. ISSN 0305-1048
Abstract
We have determined the structure of a catalytically inactive D70N variant of the Escherichia coli RusA resolvase bound to a duplex DNA substrate that reveals critical protein–DNA interactions and permits a much clearer understanding of the interaction of the enzyme with a Holliday junction (HJ). The RusA enzyme cleaves HJs, the fourway DNA branchpoints formed by homologous recombination, by introducing symmetrical cuts in the phosphodiester backbone in a Mg2+ dependent reaction. Although, RusA shows a high level of selectivity for DNA junctions, preferring to bind fourway junctions over other substrates in vitro, it has also been shown to have appreciable affinity for duplex DNA. However, RusA does not show DNA cleavage activity with duplex substrates. Our structure suggests the possible basis for structural selectivity as well as sources of the sequence specificity observed for DNA cleavage by RusA.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2006 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
Keywords: | Stalled Replication Forks; Escherichia-Coli; Crystal-Structure; Recombination; Ruva; Sequence; Repair; RECG; Identification; Endonclease |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 14 Dec 2016 12:15 |
Last Modified: | 14 Dec 2016 12:18 |
Published Version: | http://dx.doi.org/10.1093/nar/gkl447 |
Status: | Published |
Publisher: | Oxford University Press (OUP): Policy C - Option B |
Refereed: | Yes |
Identification Number: | 10.1093/nar/gkl447 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:109272 |