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Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER

2023-04-11Artigo científico Acesso aberto
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dc.contributor.authorSeck, Anna
dc.contributor.authorDe Bonis, Salvatore
dc.contributor.authorStelter, Meike
dc.contributor.authorÖkvist, Mats
dc.contributor.authorSenarisoy, Müge
dc.contributor.authorHayek, Mohammad Rida
dc.contributor.authorLe Roy, Aline
dc.contributor.authorMartin, Lydie
dc.contributor.authorSaint-Pierre, Christine
dc.contributor.authorSilveira, Célia M.
dc.contributor.authorGasparutto, Didier
dc.contributor.authorTodorovic, Smilja
dc.contributor.authorRavanat, Jean Luc
dc.contributor.authorTimmins, Joanna
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblOxford University Press
dc.date.accessioned2023-10-03T22:19:11Z
dc.date.available2023-10-03T22:19:11Z
dc.date.issued2023-04-11
dc.descriptionPublisher Copyright: © 2023 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research.
dc.description.abstractBacterial nucleotide excision repair (NER), mediated by the UvrA, UvrB and UvrC proteins is a multistep, ATP-dependent process, that is responsible for the removal of a very wide range of chemically and structurally diverse DNA lesions. DNA damage removal is performed by UvrC, an enzyme possessing a dual endonuclease activity, capable of incising the DNA on either side of the damaged site to release a short single-stranded DNA fragment containing the lesion. Using biochemical and biophysical approaches, we have probed the oligomeric state, UvrB-and DNA-binding abilities and incision activities of wild-Type and mutant constructs of UvrC from the radiation resistant bacterium, Deinococcus radiodurans. Moreover, by combining the power of new structure prediction algorithms and experimental crystallographic data, we have assembled the first model of a complete UvrC, revealing several unexpected structural motifs and in particular, a central inactive RNase H domain acting as a platform for the surrounding domains. In this configuration, UvrC is maintained in a 'closed' inactive state that needs to undergo a major rearrangement to adopt an 'open' active state capable of performing the dual incision reaction. Taken together, this study provides important insight into the mechanism of recruitment and activation of UvrC during NER.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent19
dc.format.extent7170531
dc.identifier.doi10.1093/nar/gkad108
dc.identifier.issn0305-1048
dc.identifier.otherPURE: 72623371
dc.identifier.otherPURE UUID: aee926af-dc8f-44b0-9bb4-e6475cfb9915
dc.identifier.otherScopus: 85152244641
dc.identifier.otherPubMed: 36869664
dc.identifier.urihttp://hdl.handle.net/10362/158654
dc.identifier.urlhttps://www.scopus.com/pages/publications/85152244641
dc.language.isoeng
dc.peerreviewedyes
dc.subjectGenetics
dc.titleStructural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NERen
dc.typejournal article
degois.publication.firstPage2931
degois.publication.issue6
degois.publication.lastPage2949
degois.publication.titleNucleic Acids Research
degois.publication.volume51
dspace.entity.typePublication
rcaap.rightsopenAccess

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