Structures of the CRISPR-Cmr complex reveal mode of RNA target positioning
Adaptive immunity in bacteria involves RNA-guided surveillance complexes that use CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) proteins together with CRISPR RNAs (crRNAs) to target invasive nucleic acids for degradation. Whereas type I and type II CRISPR-Cas su...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2015-05, Vol.348 (6234), p.581-585 |
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| creator | Taylor, David W. Zhu, Yifan Staals, Raymond H. J. Kornfeld, Jack E. Shinkai, Akeo van der Oost, John Nogales, Eva Doudna, Jennifer A. |
| description | Adaptive immunity in bacteria involves RNA-guided surveillance complexes that use CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) proteins together with CRISPR RNAs (crRNAs) to target invasive nucleic acids for degradation. Whereas type I and type II CRISPR-Cas surveillance complexes target double-stranded DNA, type III complexes target single-stranded RNA. Near-atomic resolution cryo–electron microscopy reconstructions of native type III Cmr (CRISPR RAMP module) complexes in the absence and presence of target RNA reveal a helical protein arrangement that positions the crRNA for substrate binding. Thumblike β hairpins intercalate between segments of duplexed crRNA:target RNA to facilitate cleavage of the target at 6-nucleotide intervals. The Cmr complex is architecturally similar to the type I CRISPR-Cascade complex, suggesting divergent evolution of these immune systems from a common ancestor. |
| doi_str_mv | 10.1126/science.aaa4535 |
| format | Article |
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J. ; Kornfeld, Jack E. ; Shinkai, Akeo ; van der Oost, John ; Nogales, Eva ; Doudna, Jennifer A.</creator><creatorcontrib>Taylor, David W. ; Zhu, Yifan ; Staals, Raymond H. J. ; Kornfeld, Jack E. ; Shinkai, Akeo ; van der Oost, John ; Nogales, Eva ; Doudna, Jennifer A.</creatorcontrib><description>Adaptive immunity in bacteria involves RNA-guided surveillance complexes that use CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) proteins together with CRISPR RNAs (crRNAs) to target invasive nucleic acids for degradation. Whereas type I and type II CRISPR-Cas surveillance complexes target double-stranded DNA, type III complexes target single-stranded RNA. Near-atomic resolution cryo–electron microscopy reconstructions of native type III Cmr (CRISPR RAMP module) complexes in the absence and presence of target RNA reveal a helical protein arrangement that positions the crRNA for substrate binding. Thumblike β hairpins intercalate between segments of duplexed crRNA:target RNA to facilitate cleavage of the target at 6-nucleotide intervals. The Cmr complex is architecturally similar to the type I CRISPR-Cascade complex, suggesting divergent evolution of these immune systems from a common ancestor.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aaa4535</identifier><identifier>PMID: 25837515</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington: American Association for the Advancement of Science</publisher><subject>Archaea ; Bacteria ; Binding ; Electron microscopes ; Electron microscopy ; Genetics ; Immune system ; Immune systems ; Nucleic acids ; Proteins ; Ramps ; Ribonucleic acids ; Surveillance ; Thermus thermophilus ; Transcription factors ; Transmission electron microscopy</subject><ispartof>Science (American Association for the Advancement of Science), 2015-05, Vol.348 (6234), p.581-585</ispartof><rights>Copyright © 2015 American Association for the Advancement of Science</rights><rights>Copyright © 2015, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-17d97c28faa8dc8e57033f87c28881a0f1a594e2b93aac7a833c0c9a7a3112a3</citedby><cites>FETCH-LOGICAL-c519t-17d97c28faa8dc8e57033f87c28881a0f1a594e2b93aac7a833c0c9a7a3112a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24747397$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24747397$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,2884,2885,27924,27925,58017,58250</link.rule.ids></links><search><creatorcontrib>Taylor, David W.</creatorcontrib><creatorcontrib>Zhu, Yifan</creatorcontrib><creatorcontrib>Staals, Raymond H. 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| source | JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Archaea Bacteria Binding Electron microscopes Electron microscopy Genetics Immune system Immune systems Nucleic acids Proteins Ramps Ribonucleic acids Surveillance Thermus thermophilus Transcription factors Transmission electron microscopy |
| title | Structures of the CRISPR-Cmr complex reveal mode of RNA target positioning |
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