Structure and Mechanism of the CMR Complex for CRISPR-Mediated Antiviral Immunity
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 subs...
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creator | Zhang, Jing Rouillon, Christophe Kerou, Melina Reeks, Judith Brugger, Kim Graham, Shirley Reimann, Julia Cannone, Giuseppe Liu, Huanting Albers, Sonja-Verena Naismith, James H. Spagnolo, Laura White, Malcolm F. |
description | 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 endonucleolytic 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 protospacer-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.
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► EM structure of the CMR complex for viral RNA degradation has been determined ► The crRNA content of CMR has been analyzed by deep sequencing ► Target RNA cleavage by CMR is sequence dependent |
doi_str_mv | 10.1016/j.molcel.2011.12.013 |
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[Display omitted]
► EM structure of the CMR complex for viral RNA degradation has been determined ► The crRNA content of CMR has been analyzed by deep sequencing ► Target RNA cleavage by CMR is sequence dependent</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2011.12.013</identifier><identifier>PMID: 22227115</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Archaeal Proteins - chemistry ; Archaeal Proteins - isolation & purification ; Archaeal Viruses - immunology ; Base Sequence ; Cellular apoptosis susceptibility protein ; Crystal structure ; Crystallography, X-Ray ; DNA ; Immunity ; Infection ; Inverted Repeat Sequences ; Macromolecular Substances - chemistry ; Macromolecular Substances - isolation & purification ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - isolation & purification ; Ribonucleoproteins ; RNA ; RNA Cleavage ; RNA, Archaeal - chemistry ; RNA, Archaeal - genetics ; RNA, Archaeal - isolation & purification ; Sulfolobus solfataricus ; Sulfolobus solfataricus - genetics ; Sulfolobus solfataricus - immunology ; Sulfolobus solfataricus - metabolism ; Sulfolobus solfataricus - virology</subject><ispartof>Molecular cell, 2012-02, Vol.45 (3), p.303-313</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c560t-c2a9dd6425ee199b9a17d0a054c96c61d95f00e425cd9ea037ff0cf228af82903</citedby><cites>FETCH-LOGICAL-c560t-c2a9dd6425ee199b9a17d0a054c96c61d95f00e425cd9ea037ff0cf228af82903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molcel.2011.12.013$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22227115$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Jing</creatorcontrib><creatorcontrib>Rouillon, Christophe</creatorcontrib><creatorcontrib>Kerou, Melina</creatorcontrib><creatorcontrib>Reeks, Judith</creatorcontrib><creatorcontrib>Brugger, Kim</creatorcontrib><creatorcontrib>Graham, Shirley</creatorcontrib><creatorcontrib>Reimann, Julia</creatorcontrib><creatorcontrib>Cannone, Giuseppe</creatorcontrib><creatorcontrib>Liu, Huanting</creatorcontrib><creatorcontrib>Albers, Sonja-Verena</creatorcontrib><creatorcontrib>Naismith, James H.</creatorcontrib><creatorcontrib>Spagnolo, Laura</creatorcontrib><creatorcontrib>White, Malcolm F.</creatorcontrib><title>Structure and Mechanism of the CMR Complex for CRISPR-Mediated Antiviral Immunity</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>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 endonucleolytic 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 protospacer-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.
[Display omitted]
► EM structure of the CMR complex for viral RNA degradation has been determined ► The crRNA content of CMR has been analyzed by deep sequencing ► Target RNA cleavage by CMR is sequence dependent</description><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - isolation & purification</subject><subject>Archaeal Viruses - immunology</subject><subject>Base Sequence</subject><subject>Cellular apoptosis susceptibility protein</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>Immunity</subject><subject>Infection</subject><subject>Inverted Repeat Sequences</subject><subject>Macromolecular Substances - chemistry</subject><subject>Macromolecular Substances - isolation & purification</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - isolation & purification</subject><subject>Ribonucleoproteins</subject><subject>RNA</subject><subject>RNA Cleavage</subject><subject>RNA, Archaeal - chemistry</subject><subject>RNA, Archaeal - genetics</subject><subject>RNA, Archaeal - isolation & purification</subject><subject>Sulfolobus solfataricus</subject><subject>Sulfolobus solfataricus - genetics</subject><subject>Sulfolobus solfataricus - immunology</subject><subject>Sulfolobus solfataricus - metabolism</subject><subject>Sulfolobus solfataricus - virology</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EoqXwDRDyjVPC2HH--IJURQVW6grYwtly7QnrVRIvtrOi3x5XuxS4gC-2NG-eZ96PkJcMSgasebMrJz8aHEsOjJWMl8CqR-ScgWwLwRrx-PTmbVOfkWcx7gCYqDv5lJzxfFrG6nPy-SaFxaQlINWzpWs0Wz27OFE_0LRF2q83tPfTfsQfdPCB9pvVzadNsUbrdEJLL-fkDi7oka6maZlduntOngx6jPjidF-Qr--uvvQfiuuP71f95XVh6gZSYbiW1jaC14hMylupWWtBQy2MbEzDrKwHAMx1YyVqqNphADNw3umh4xKqC_L26Ltfbie0BueUx1D74CYd7pTXTv1dmd1WffMHVVUd60SbDV6fDIL_vmBManIxBzrqGf0SlaxFIwA6-L-SM5EDhTorxVFpgo8x4PAwDwN1j03t1BGbusemGFcZW2579ecuD02_OP1eFnOiB4dBReNwNhlDQJOU9e7fP_wEDuuq7Q</recordid><startdate>20120210</startdate><enddate>20120210</enddate><creator>Zhang, Jing</creator><creator>Rouillon, Christophe</creator><creator>Kerou, Melina</creator><creator>Reeks, Judith</creator><creator>Brugger, Kim</creator><creator>Graham, Shirley</creator><creator>Reimann, Julia</creator><creator>Cannone, Giuseppe</creator><creator>Liu, Huanting</creator><creator>Albers, Sonja-Verena</creator><creator>Naismith, James H.</creator><creator>Spagnolo, Laura</creator><creator>White, Malcolm F.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7T5</scope><scope>7U9</scope><scope>H94</scope><scope>5PM</scope></search><sort><creationdate>20120210</creationdate><title>Structure and Mechanism of the CMR Complex for CRISPR-Mediated Antiviral Immunity</title><author>Zhang, Jing ; Rouillon, Christophe ; Kerou, Melina ; Reeks, Judith ; Brugger, Kim ; Graham, Shirley ; Reimann, Julia ; Cannone, Giuseppe ; Liu, Huanting ; Albers, Sonja-Verena ; Naismith, James H. ; Spagnolo, Laura ; White, Malcolm F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c560t-c2a9dd6425ee199b9a17d0a054c96c61d95f00e425cd9ea037ff0cf228af82903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - isolation & purification</topic><topic>Archaeal Viruses - immunology</topic><topic>Base Sequence</topic><topic>Cellular apoptosis susceptibility protein</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>Immunity</topic><topic>Infection</topic><topic>Inverted Repeat Sequences</topic><topic>Macromolecular Substances - chemistry</topic><topic>Macromolecular Substances - isolation & purification</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - isolation & purification</topic><topic>Ribonucleoproteins</topic><topic>RNA</topic><topic>RNA Cleavage</topic><topic>RNA, Archaeal - chemistry</topic><topic>RNA, Archaeal - genetics</topic><topic>RNA, Archaeal - isolation & purification</topic><topic>Sulfolobus solfataricus</topic><topic>Sulfolobus solfataricus - genetics</topic><topic>Sulfolobus solfataricus - immunology</topic><topic>Sulfolobus solfataricus - metabolism</topic><topic>Sulfolobus solfataricus - virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Jing</creatorcontrib><creatorcontrib>Rouillon, Christophe</creatorcontrib><creatorcontrib>Kerou, Melina</creatorcontrib><creatorcontrib>Reeks, Judith</creatorcontrib><creatorcontrib>Brugger, Kim</creatorcontrib><creatorcontrib>Graham, Shirley</creatorcontrib><creatorcontrib>Reimann, Julia</creatorcontrib><creatorcontrib>Cannone, Giuseppe</creatorcontrib><creatorcontrib>Liu, Huanting</creatorcontrib><creatorcontrib>Albers, Sonja-Verena</creatorcontrib><creatorcontrib>Naismith, James H.</creatorcontrib><creatorcontrib>Spagnolo, Laura</creatorcontrib><creatorcontrib>White, Malcolm F.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Jing</au><au>Rouillon, Christophe</au><au>Kerou, Melina</au><au>Reeks, Judith</au><au>Brugger, Kim</au><au>Graham, Shirley</au><au>Reimann, Julia</au><au>Cannone, Giuseppe</au><au>Liu, Huanting</au><au>Albers, Sonja-Verena</au><au>Naismith, James H.</au><au>Spagnolo, Laura</au><au>White, Malcolm F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and Mechanism of the CMR Complex for CRISPR-Mediated Antiviral Immunity</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2012-02-10</date><risdate>2012</risdate><volume>45</volume><issue>3</issue><spage>303</spage><epage>313</epage><pages>303-313</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><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 endonucleolytic 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 protospacer-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.
[Display omitted]
► EM structure of the CMR complex for viral RNA degradation has been determined ► The crRNA content of CMR has been analyzed by deep sequencing ► Target RNA cleavage by CMR is sequence dependent</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22227115</pmid><doi>10.1016/j.molcel.2011.12.013</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Archaeal Proteins - chemistry Archaeal Proteins - isolation & purification Archaeal Viruses - immunology Base Sequence Cellular apoptosis susceptibility protein Crystal structure Crystallography, X-Ray DNA Immunity Infection Inverted Repeat Sequences Macromolecular Substances - chemistry Macromolecular Substances - isolation & purification Microscopy, Electron Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - isolation & purification Ribonucleoproteins RNA RNA Cleavage RNA, Archaeal - chemistry RNA, Archaeal - genetics RNA, Archaeal - isolation & purification Sulfolobus solfataricus Sulfolobus solfataricus - genetics Sulfolobus solfataricus - immunology Sulfolobus solfataricus - metabolism Sulfolobus solfataricus - virology |
title | Structure and Mechanism of the CMR Complex for CRISPR-Mediated Antiviral Immunity |
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