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Structure and mechanism of the CMR complex for CRISPR-Mediated antiviral immunity
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dc.contributor.author | Zhang, Jing | |
dc.contributor.author | Rouillon, Christophe | |
dc.contributor.author | Kerou, Melina | |
dc.contributor.author | Reeks, Judith | |
dc.contributor.author | Brugger, Kim | |
dc.contributor.author | Graham, Shirley | |
dc.contributor.author | Reimann, Julia | |
dc.contributor.author | Cannone, Giuseppe | |
dc.contributor.author | Liu, Huanting | |
dc.contributor.author | Albers, Sonja-Verena | |
dc.contributor.author | Naismith, James H. | |
dc.contributor.author | Spagnolo, Laura | |
dc.contributor.author | White, Malcolm F | |
dc.date.accessioned | 2015-01-13T12:01:02Z | |
dc.date.available | 2015-01-13T12:01:02Z | |
dc.date.issued | 2012-02-10 | |
dc.identifier.citation | Zhang , J , Rouillon , C , Kerou , M , Reeks , J , Brugger , K , Graham , S , Reimann , J , Cannone , G , Liu , H , Albers , S-V , Naismith , J H , Spagnolo , L & White , M F 2012 , ' Structure and mechanism of the CMR complex for CRISPR-Mediated antiviral immunity ' , Molecular Cell , vol. 45 , no. 3 , pp. 303-313 . https://doi.org/10.1016/j.molcel.2011.12.013 | en |
dc.identifier.issn | 1097-2765 | |
dc.identifier.other | PURE: 18094393 | |
dc.identifier.other | PURE UUID: c54d238d-c149-4bf1-ad45-591bcd8e34ec | |
dc.identifier.other | WOS: 000300481100006 | |
dc.identifier.other | Scopus: 84856778250 | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/47136090 | |
dc.identifier.uri | https://hdl.handle.net/10023/5991 | |
dc.description.abstract | The prokaryotic clusters of regularly interspaced palindromic repeats (CRISPR) system utilizes genomically encoded CRISPR RNA (crRNA), derived from invading viruses and incorporated into ribonucleoprotein complexes with CRISPR-associated (CAS) proteins, to target and degrade viral DNA or RNA on subsequent infection. RNA is targeted by the CMR complex. In Sulfolobus solfataricus, this complex is composed of seven CAS protein subunits (Cmr1-7) and carries a diverse "payload" of targeting crRNA. The crystal structure of Cmr7 and low-resolution structure of the complex are presented. S. solfataricus CMR cleaves RNA targets in an endo-nucleolytic reaction at UA dinucleotides. This activity is dependent on the 8 nt repeat-derived 5' sequence in the crRNA, but not on the presence of a proto-spacer-associated motif (PAM) in the target. Both target and guide RNAs can be cleaved, although a single molecule of guide RNA can support the degradation of multiple targets. | |
dc.format.extent | 11 | |
dc.language.iso | eng | |
dc.relation.ispartof | Molecular Cell | en |
dc.rights | (c)2012 Elsevier Inc. This article is available under an Elsevier user license which allows re-use for non-commercial purposes. See http://www.elsevier.com/about/open-access/open-access-policies/oa-license-policy/elsevier-user-license | en |
dc.subject | QR355 Virology | en |
dc.subject.lcc | QR355 | en |
dc.title | Structure and mechanism of the CMR complex for CRISPR-Mediated antiviral immunity | en |
dc.type | Journal article | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | BBSRC | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.identifier.doi | https://doi.org/10.1016/j.molcel.2011.12.013 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | http://ukpmc.ac.uk/articles/PMC3381847 | en |
dc.identifier.grantnumber | BBS/B/14426 | en |
dc.identifier.grantnumber | BB/G011400/1 | en |
dc.identifier.grantnumber | BBS/B/14426 | en |
dc.identifier.grantnumber | BB/G011400/1 | en |
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