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dc.contributor.authorReeks, Judith Anne
dc.contributor.authorNaismith, Jim
dc.contributor.authorWhite, Malcolm F
dc.date.accessioned2013-07-23T14:01:01Z
dc.date.available2013-07-23T14:01:01Z
dc.date.issued2013-06
dc.identifier.citationReeks , J A , Naismith , J & White , M F 2013 , ' CRISPR interference : a structural perspective ' Biochemical Journal , vol. 453 , no. 2 , pp. 155-166 . DOI: 10.1042/BJ20130316en
dc.identifier.issn0264-6021
dc.identifier.otherPURE: 60328306
dc.identifier.otherPURE UUID: 551e7684-6284-47a3-955e-27147e9703c2
dc.identifier.otherWOS: 000321808800001
dc.identifier.otherScopus: 84879584456
dc.identifier.urihttp://hdl.handle.net/10023/3863
dc.descriptionThis article was made open access through BIS OA funding. The laboratory is funded by grants from the Biotechnology and Biological Sciences Research Council (BBSRC).en
dc.description.abstractCRISPR (cluster of regularly interspaced palindromic repeats) is a prokaryotic adaptive defence system, providing immunity against mobile genetic elements such as viruses. Genomically encoded crRNA (CRISPR RNA) is used by Cas (CRISPR-associated) proteins to target and subsequently degrade nucleic acids of invading entities in a sequence-dependent manner. The process is known as ‘interference’. In the present review we cover recent progress on the structural biology of the CRISPR/Cas system, focusing on the Cas proteins and complexes that catalyse crRNA biogenesis and interference. Structural studies have helped in the elucidation of key mechanisms, including the recognition and cleavage of crRNA by the Cas6 and Cas5 proteins, where remarkable diversity at the level of both substrate recognition and catalysis has become apparent. The RNA-binding RAMP (repeat-associated mysterious protein) domain is present in the Cas5, Cas6, Cas7 and Cmr3 protein families and RAMP-like domains are found in Cas2 and Cas10. Structural analysis has also revealed an evolutionary link between the small subunits of the type I and type III-B interference complexes. Future studies of the interference complexes and their constituent components will transform our understanding of the system.en
dc.format.extent12en
dc.language.isoeng
dc.relation.ispartofBiochemical Journalen
dc.rights© 2013 The Authors. The authors have paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.en
dc.subjectAntiviral defenceen
dc.subjectCluster of regularly interspaced palindromic repeats (CRISPR)en
dc.subjectCrystallographyen
dc.subjectEvolutionen
dc.subjectProtein structureen
dc.subjectRepeat-associated mysterious protein (RAMP)en
dc.subjectQ Scienceen
dc.subject.lccQen
dc.titleCRISPR interference : a structural perspectiveen
dc.typeJournal itemen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1042/BJ20130316
dc.description.statusPeer revieweden


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