Substrate affinity and substrate specificity of proteasomes with RNase activity
We have partially reconstituted 20S proteasome/RNA complexes using oligonucleotides corresponding to ARE (adenosine- and uridine-rich element) (AUUUA)4 and HIV-TAR (human immunodeficiency virus-Tat transactivation response element), a stem-loop structure in the 5' UTR (untranslated region) of H...
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| Veröffentlicht in: | Molecular biology reports 2003-03, Vol.30 (1), p.1-7 |
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| creator | Gautier-Bert, Karine Murol, Bertrand Jarrousse, Anne-Sophie Ballut, Lionel Badaoui, Saloua Petit, Frank Schmid, Hans-Peter |
| description | We have partially reconstituted 20S proteasome/RNA complexes using oligonucleotides corresponding to ARE (adenosine- and uridine-rich element) (AUUUA)4 and HIV-TAR (human immunodeficiency virus-Tat transactivation response element), a stem-loop structure in the 5' UTR (untranslated region) of HIV-mRNAs. We demonstrate that these RNAs which associate with proteasomes are degraded by proteasomal endonuclease activity. The formation of these 20S proteasome/RNA substrate complexes is rather specific since 20S proteasomes do not interfere with truncated TAR that is not cleaved by proteasomal endonuclease. In addition, affinity of proteasomes for (AUUUA)4 is much stronger as it is for HIV-TAR. These results provide further arguments for our hypothesis that proteasomes could be involved in the destabilisation of cytokines mRNAs containing AUUUA sequences as well as viral mRNAs. |
| doi_str_mv | 10.1023/A:1022261925117 |
| format | Article |
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We demonstrate that these RNAs which associate with proteasomes are degraded by proteasomal endonuclease activity. The formation of these 20S proteasome/RNA substrate complexes is rather specific since 20S proteasomes do not interfere with truncated TAR that is not cleaved by proteasomal endonuclease. In addition, affinity of proteasomes for (AUUUA)4 is much stronger as it is for HIV-TAR. These results provide further arguments for our hypothesis that proteasomes could be involved in the destabilisation of cytokines mRNAs containing AUUUA sequences as well as viral mRNAs.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1023/A:1022261925117</identifier><identifier>PMID: 12688529</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Animals ; Cattle ; Cysteine Endopeptidases - metabolism ; HIV Long Terminal Repeat - physiology ; HIV-1 - genetics ; HIV-1 - metabolism ; Multienzyme Complexes - metabolism ; Proteasome Endopeptidase Complex ; Proteins ; Ribonucleases - metabolism ; RNA, Messenger - metabolism ; Substrate Specificity</subject><ispartof>Molecular biology reports, 2003-03, Vol.30 (1), p.1-7</ispartof><rights>Kluwer Academic Publishers 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c311t-8de505b2a8e5ff7eb8fdfe7dbfe0460b20c968c6744c8bbced158d6aef89a9cd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12688529$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gautier-Bert, Karine</creatorcontrib><creatorcontrib>Murol, Bertrand</creatorcontrib><creatorcontrib>Jarrousse, Anne-Sophie</creatorcontrib><creatorcontrib>Ballut, Lionel</creatorcontrib><creatorcontrib>Badaoui, Saloua</creatorcontrib><creatorcontrib>Petit, Frank</creatorcontrib><creatorcontrib>Schmid, Hans-Peter</creatorcontrib><title>Substrate affinity and substrate specificity of proteasomes with RNase activity</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><description>We have partially reconstituted 20S proteasome/RNA complexes using oligonucleotides corresponding to ARE (adenosine- and uridine-rich element) (AUUUA)4 and HIV-TAR (human immunodeficiency virus-Tat transactivation response element), a stem-loop structure in the 5' UTR (untranslated region) of HIV-mRNAs. We demonstrate that these RNAs which associate with proteasomes are degraded by proteasomal endonuclease activity. The formation of these 20S proteasome/RNA substrate complexes is rather specific since 20S proteasomes do not interfere with truncated TAR that is not cleaved by proteasomal endonuclease. In addition, affinity of proteasomes for (AUUUA)4 is much stronger as it is for HIV-TAR. These results provide further arguments for our hypothesis that proteasomes could be involved in the destabilisation of cytokines mRNAs containing AUUUA sequences as well as viral mRNAs.</description><subject>Animals</subject><subject>Cattle</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>HIV Long Terminal Repeat - physiology</subject><subject>HIV-1 - genetics</subject><subject>HIV-1 - metabolism</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Proteins</subject><subject>Ribonucleases - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Substrate Specificity</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqF0DtLA0EQAOBFFBOjtZ0cFnanO7u3L7sQfEEw4KM-9okbcrl4u6fk33vio7CxGpj5ZpgZhI4BnwMm9GJ6OQRCOCjCAMQOGgMTtKyUkLtojCmGspIMRuggpSXGuALB9tEICJeSETVGi8fepNzp7AsdQlzHvC302hXpN5023sYQ7WelDcWma7PXqW18Kt5jfike7nUamm2ObwM5RHtBr5I_-o4T9Hx99TS7LeeLm7vZdF5aCpBL6TzDzBAtPQtBeCODC144EzyuODYEW8Wl5aKqrDTGegdMOq59kEor6-gEnX3NHfZ57X3KdROT9auVXvu2T7WgoAAw_AtBci4EyAGe_oHLtu_WwxG1qKgSSikyoJNv1JvGu3rTxUZ32_rnofQDVl15Jg</recordid><startdate>200303</startdate><enddate>200303</enddate><creator>Gautier-Bert, Karine</creator><creator>Murol, Bertrand</creator><creator>Jarrousse, Anne-Sophie</creator><creator>Ballut, Lionel</creator><creator>Badaoui, Saloua</creator><creator>Petit, Frank</creator><creator>Schmid, Hans-Peter</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>200303</creationdate><title>Substrate affinity and substrate specificity of proteasomes with RNase activity</title><author>Gautier-Bert, Karine ; Murol, Bertrand ; Jarrousse, Anne-Sophie ; Ballut, Lionel ; Badaoui, Saloua ; Petit, Frank ; Schmid, Hans-Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311t-8de505b2a8e5ff7eb8fdfe7dbfe0460b20c968c6744c8bbced158d6aef89a9cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Cysteine Endopeptidases - 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Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gautier-Bert, Karine</au><au>Murol, Bertrand</au><au>Jarrousse, Anne-Sophie</au><au>Ballut, Lionel</au><au>Badaoui, Saloua</au><au>Petit, Frank</au><au>Schmid, Hans-Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate affinity and substrate specificity of proteasomes with RNase activity</atitle><jtitle>Molecular biology reports</jtitle><addtitle>Mol Biol Rep</addtitle><date>2003-03</date><risdate>2003</risdate><volume>30</volume><issue>1</issue><spage>1</spage><epage>7</epage><pages>1-7</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>We have partially reconstituted 20S proteasome/RNA complexes using oligonucleotides corresponding to ARE (adenosine- and uridine-rich element) (AUUUA)4 and HIV-TAR (human immunodeficiency virus-Tat transactivation response element), a stem-loop structure in the 5' UTR (untranslated region) of HIV-mRNAs. 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| subjects | Animals Cattle Cysteine Endopeptidases - metabolism HIV Long Terminal Repeat - physiology HIV-1 - genetics HIV-1 - metabolism Multienzyme Complexes - metabolism Proteasome Endopeptidase Complex Proteins Ribonucleases - metabolism RNA, Messenger - metabolism Substrate Specificity |
| title | Substrate affinity and substrate specificity of proteasomes with RNase activity |
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