The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES
Picornavirus mRNAs contain IRESs that sustain their translation during infection, when host protein synthesis is shut off. The major classes of picornavirus IRESs (Types 1 and 2) have distinct structures and sequences, but initiation on both is determined by their specific interaction with eIF4G. We...
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description | Picornavirus mRNAs contain IRESs that sustain their translation during infection, when host protein synthesis is shut off. The major classes of picornavirus IRESs (Types 1 and 2) have distinct structures and sequences, but initiation on both is determined by their specific interaction with eIF4G. We report here that Aichivirus (AV), a member of the Kobuvirus genus of
Picornaviridae
, contains an IRES that differs structurally from Type 1 and Type 2 IRESs. Its function similarly involves interaction with eIF4G, but its eIF4G‐interacting domain is structurally distinct, although it contains an apical eIF4G‐interacting motif similar to that in Type 2 IRESs. Like Type 1 and Type 2 IRESs, AV IRES function is enhanced by pyrimidine tract‐binding protein (PTB), but the pattern of PTB's interaction with each of these IRESs is distinct. Unlike all known IRESs, the AV IRES is absolutely dependent on DHX29, a requirement imposed by sequestration of its initiation codon in a stable hairpin.
Picornavirus mRNAs contain internal ribosomal entry sites (IRESs) that mediate translation during infection, when global host protein synthesis is inhibited. Aichi Virus harbours a novel type of IRES that needs the DExH‐box helicase DHX29 for function. |
doi_str_mv | 10.1038/emboj.2011.306 |
format | Article |
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Picornaviridae
, contains an IRES that differs structurally from Type 1 and Type 2 IRESs. Its function similarly involves interaction with eIF4G, but its eIF4G‐interacting domain is structurally distinct, although it contains an apical eIF4G‐interacting motif similar to that in Type 2 IRESs. Like Type 1 and Type 2 IRESs, AV IRES function is enhanced by pyrimidine tract‐binding protein (PTB), but the pattern of PTB's interaction with each of these IRESs is distinct. Unlike all known IRESs, the AV IRES is absolutely dependent on DHX29, a requirement imposed by sequestration of its initiation codon in a stable hairpin.
Picornavirus mRNAs contain internal ribosomal entry sites (IRESs) that mediate translation during infection, when global host protein synthesis is inhibited. Aichi Virus harbours a novel type of IRES that needs the DExH‐box helicase DHX29 for function.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2011.306</identifier><identifier>PMID: 21873976</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>5' Untranslated Regions - genetics ; Aichivirus ; Base Sequence ; Binding Sites - genetics ; DHX29 ; eIF4G ; EMBO23 ; EMBO31 ; Gene Expression Regulation, Viral ; IRES ; Kobuvirus - genetics ; Models, Molecular ; Molecular biology ; Molecular Sequence Data ; Nucleic Acid Conformation ; Peptide Chain Initiation, Translational - genetics ; Picornaviridae ; Picornaviridae - genetics ; Picornaviridae - metabolism ; Picornavirus ; Protein Biosynthesis - genetics ; Protein Biosynthesis - physiology ; Protein synthesis ; PTB ; Regulatory Elements, Transcriptional - genetics ; Regulatory Elements, Transcriptional - physiology ; Ribonucleic acid ; Ribosomes - metabolism ; RNA ; RNA, Viral - chemistry ; RNA, Viral - genetics ; RNA, Viral - metabolism ; Viruses</subject><ispartof>The EMBO journal, 2011-11, Vol.30 (21), p.4423-4436</ispartof><rights>European Molecular Biology Organization 2011</rights><rights>Copyright © 2011 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Nov 2, 2011</rights><rights>Copyright © 2011, European Molecular Biology Organization 2011 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6296-af1c632f39fffd1a2a318c7fd5bbe399627f5a981fafcef0b0ff374dad6e1f6f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3230369/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3230369/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,1418,1434,27929,27930,41125,42194,45579,45580,46414,46838,51581,53796,53798</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2011.306$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21873976$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Yingpu</creatorcontrib><creatorcontrib>Sweeney, Trevor R</creatorcontrib><creatorcontrib>Kafasla, Panagiota</creatorcontrib><creatorcontrib>Jackson, Richard J</creatorcontrib><creatorcontrib>Pestova, Tatyana V</creatorcontrib><creatorcontrib>Hellen, Christopher UT</creatorcontrib><title>The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Picornavirus mRNAs contain IRESs that sustain their translation during infection, when host protein synthesis is shut off. The major classes of picornavirus IRESs (Types 1 and 2) have distinct structures and sequences, but initiation on both is determined by their specific interaction with eIF4G. We report here that Aichivirus (AV), a member of the Kobuvirus genus of
Picornaviridae
, contains an IRES that differs structurally from Type 1 and Type 2 IRESs. Its function similarly involves interaction with eIF4G, but its eIF4G‐interacting domain is structurally distinct, although it contains an apical eIF4G‐interacting motif similar to that in Type 2 IRESs. Like Type 1 and Type 2 IRESs, AV IRES function is enhanced by pyrimidine tract‐binding protein (PTB), but the pattern of PTB's interaction with each of these IRESs is distinct. Unlike all known IRESs, the AV IRES is absolutely dependent on DHX29, a requirement imposed by sequestration of its initiation codon in a stable hairpin.
Picornavirus mRNAs contain internal ribosomal entry sites (IRESs) that mediate translation during infection, when global host protein synthesis is inhibited. Aichi Virus harbours a novel type of IRES that needs the DExH‐box helicase DHX29 for function.</description><subject>5' Untranslated Regions - genetics</subject><subject>Aichivirus</subject><subject>Base Sequence</subject><subject>Binding Sites - genetics</subject><subject>DHX29</subject><subject>eIF4G</subject><subject>EMBO23</subject><subject>EMBO31</subject><subject>Gene Expression Regulation, Viral</subject><subject>IRES</subject><subject>Kobuvirus - genetics</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Peptide Chain Initiation, Translational - genetics</subject><subject>Picornaviridae</subject><subject>Picornaviridae - genetics</subject><subject>Picornaviridae - metabolism</subject><subject>Picornavirus</subject><subject>Protein Biosynthesis - genetics</subject><subject>Protein Biosynthesis - physiology</subject><subject>Protein synthesis</subject><subject>PTB</subject><subject>Regulatory Elements, Transcriptional - genetics</subject><subject>Regulatory Elements, Transcriptional - physiology</subject><subject>Ribonucleic acid</subject><subject>Ribosomes - metabolism</subject><subject>RNA</subject><subject>RNA, Viral - chemistry</subject><subject>RNA, Viral - genetics</subject><subject>RNA, Viral - metabolism</subject><subject>Viruses</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9ktFv0zAQxi0EYmXwyiOKeIGXdHYuseMXpG7qxqZtSGOIvVlOYrcuiV3ipKP_Pc4yWkAIyZJt3e_77nw-hF4TPCUY8iPVFG41TTAhU8D0CZqQlOI4wSx7iiY4oSROSc4P0AvvVxjjLGfkOTpISM6AMzpBi9ulihpVLqU1vomcjrpWWl_LzjgbGWs6Mx7DmplyaTam7X10cz0LqirEVBUV20hG1m1UHXXbtRpM1qZ0rZUjfH4z__wSPdOy9urV436IvpzOb08-xpefzs5PZpdxSRNOY6lJSSHRwLXWFZGJBJKXTFdZUSjgnCZMZ5LnREtdKo0LrDWwtJIVVURTDYfow-i77otQYKlseE8t1q1pZLsVThrxZ8SapVi4jYAEMFAeDN49GrTue698JxrjS1XX0irXe8FxAilANpDv_0sSjPMcQtPTgL79C125PvSnHvwyzAHw4Pfm99J3Nf_6rACwEbg3tdru4gSLYRTEwyiIYRREGAUxvzq-GC7hHJRHo9IHkV2odp__3-p9xVZ2fat2yR6wvW08QsZ36seOke03QRmwTHy9PhPZRXbF7jgRd_ATm8nUFg</recordid><startdate>20111102</startdate><enddate>20111102</enddate><creator>Yu, Yingpu</creator><creator>Sweeney, Trevor R</creator><creator>Kafasla, Panagiota</creator><creator>Jackson, Richard J</creator><creator>Pestova, Tatyana V</creator><creator>Hellen, Christopher UT</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20111102</creationdate><title>The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES</title><author>Yu, Yingpu ; Sweeney, Trevor R ; Kafasla, Panagiota ; Jackson, Richard J ; Pestova, Tatyana V ; Hellen, Christopher UT</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6296-af1c632f39fffd1a2a318c7fd5bbe399627f5a981fafcef0b0ff374dad6e1f6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>5' Untranslated Regions - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Yu, Yingpu</au><au>Sweeney, Trevor R</au><au>Kafasla, Panagiota</au><au>Jackson, Richard J</au><au>Pestova, Tatyana V</au><au>Hellen, Christopher UT</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2011-11-02</date><risdate>2011</risdate><volume>30</volume><issue>21</issue><spage>4423</spage><epage>4436</epage><pages>4423-4436</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Picornavirus mRNAs contain IRESs that sustain their translation during infection, when host protein synthesis is shut off. The major classes of picornavirus IRESs (Types 1 and 2) have distinct structures and sequences, but initiation on both is determined by their specific interaction with eIF4G. We report here that Aichivirus (AV), a member of the Kobuvirus genus of
Picornaviridae
, contains an IRES that differs structurally from Type 1 and Type 2 IRESs. Its function similarly involves interaction with eIF4G, but its eIF4G‐interacting domain is structurally distinct, although it contains an apical eIF4G‐interacting motif similar to that in Type 2 IRESs. Like Type 1 and Type 2 IRESs, AV IRES function is enhanced by pyrimidine tract‐binding protein (PTB), but the pattern of PTB's interaction with each of these IRESs is distinct. Unlike all known IRESs, the AV IRES is absolutely dependent on DHX29, a requirement imposed by sequestration of its initiation codon in a stable hairpin.
Picornavirus mRNAs contain internal ribosomal entry sites (IRESs) that mediate translation during infection, when global host protein synthesis is inhibited. Aichi Virus harbours a novel type of IRES that needs the DExH‐box helicase DHX29 for function.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>21873976</pmid><doi>10.1038/emboj.2011.306</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 5' Untranslated Regions - genetics Aichivirus Base Sequence Binding Sites - genetics DHX29 eIF4G EMBO23 EMBO31 Gene Expression Regulation, Viral IRES Kobuvirus - genetics Models, Molecular Molecular biology Molecular Sequence Data Nucleic Acid Conformation Peptide Chain Initiation, Translational - genetics Picornaviridae Picornaviridae - genetics Picornaviridae - metabolism Picornavirus Protein Biosynthesis - genetics Protein Biosynthesis - physiology Protein synthesis PTB Regulatory Elements, Transcriptional - genetics Regulatory Elements, Transcriptional - physiology Ribonucleic acid Ribosomes - metabolism RNA RNA, Viral - chemistry RNA, Viral - genetics RNA, Viral - metabolism Viruses |
title | The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES |
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