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dc.contributor.authorZhu, Wenlong
dc.contributor.authorMcQuarrie, Stuart John
dc.contributor.authorGruschow, Sabine
dc.contributor.authorMcMahon, Stephen
dc.contributor.authorGraham, Shirley
dc.contributor.authorGloster, Tracey
dc.contributor.authorWhite, Malcolm
dc.date.accessioned2021-02-17T16:30:12Z
dc.date.available2021-02-17T16:30:12Z
dc.date.issued2021-03-18
dc.identifier.citationZhu , W , McQuarrie , S J , Gruschow , S , McMahon , S , Graham , S , Gloster , T & White , M 2021 , ' The CRISPR ancillary effector Can2 is a dual-specificity nuclease potentiating type III CRISPR defence ' , Nucleic Acids Research , vol. 49 , no. 5 , gkab073 , pp. 2777–2789 . https://doi.org/10.1093/nar/gkab073en
dc.identifier.issn0305-1048
dc.identifier.otherPURE: 272564053
dc.identifier.otherPURE UUID: 2865bdf7-be59-4b46-a155-58951db4c3fb
dc.identifier.otherORCID: /0000-0003-1543-9342/work/89178131
dc.identifier.otherScopus: 85103229027
dc.identifier.otherWOS: 000637321700030
dc.identifier.urihttp://hdl.handle.net/10023/21442
dc.descriptionFunding: Biotechnology and Biological Sciences Research Council [BB/S000313/1 to M.F.W., BB/T004789/1 to M.F.W. and T.M.G.]; Wellcome Trust Institutional Strategic Support Funding [204821/Z/16/Z to M.F.W. and T.M.G.]; China Scholarship Council [201703780015 to W.Z.]. Funding for open access charge: RCUK block grant.en
dc.description.abstractCells and organisms have a wide range of mechanisms to defend against infection by viruses and other mobile genetic elements (MGE). Type III CRISPR systems detect foreign RNA and typically generate cyclic oligoadenylate (cOA) second messengers that bind to ancillary proteins with CARF (CRISPR associated Rossman fold) domains. This results in the activation of fused effector domains for antiviral defence. The best characterised CARF family effectors are the Csm6/Csx1 ribonucleases and DNA nickase Can1. Here we investigate a widely distributed CARF family effector with a nuclease domain, which we name Can2 (CRISPR ancillary nuclease 2). Can2 is activated by cyclic tetra-adenylate (cA4) and displays both DNase and RNase activity, providing effective immunity against plasmid transformation and bacteriophage infection in Escherichia coli. The structure of Can2 in complex with cA4 suggests a mechanism for the cA4-mediated activation of the enzyme, whereby an active site cleft is exposed on binding the activator. These findings extend our understanding of type III CRISPR cOA signalling and effector function.
dc.format.extent13
dc.language.isoeng
dc.relation.ispartofNucleic Acids Researchen
dc.rightsCopyright The Author(s) 2021. 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 License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectQH301 Biologyen
dc.subjectQH426 Geneticsen
dc.subjectDASen
dc.subject.lccQH301en
dc.subject.lccQH426en
dc.titleThe CRISPR ancillary effector Can2 is a dual-specificity nuclease potentiating type III CRISPR defenceen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.St Andrews Bioinformatics Uniten
dc.identifier.doihttps://doi.org/10.1093/nar/gkab073
dc.description.statusPeer revieweden
dc.identifier.urlhttps://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkab073/6137369?searchresult=1en


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