The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1
The transcriptional coactivator OBF‐1, which interacts with Oct‐1 and Oct‐2 and the octamer site DNA, has been shown to be critical for development of a normal immune response and the formation of germinal centers in secondary lymphoid organs. Here we have identified the RING finger protein Siah‐1 a...
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| creator | Tiedt, Ralph Bartholdy, Boris A. Matthias, Gabriele Newell, John W. Matthias, Patrick |
| description | The transcriptional coactivator OBF‐1, which interacts with Oct‐1 and Oct‐2 and the octamer site DNA, has been shown to be critical for development of a normal immune response and the formation of germinal centers in secondary lymphoid organs. Here we have identified the RING finger protein Siah‐1 as a protein interacting specifically with OBF‐1. This interaction is mediated by the C‐terminal part of Siah‐1 and by residues in the N‐terminus of OBF‐1, partly distinct from the residues required for formation of a complex with the Oct POU domains and the DNA. Interaction between Siah‐1 and OBF‐1 leads to downregulation of OBF‐1 protein level but not mRNA, and to a corresponding reduction in octamer site‐dependent transcription activation. Inhibition of the ubiquitin‐proteasome pathway in B cells leads to elevated levels of OBF‐1 protein. Furthermore, in immunized mice, OBF‐1 protein amounts are dramatically increased in primary activated B cells, without concomitant increase in OBF‐1 mRNA. These data suggest that Siah‐1 is part of a novel regulatory loop controlling the level of OBF‐1 protein in B cells. |
| doi_str_mv | 10.1093/emboj/20.15.4143 |
| format | Article |
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Here we have identified the RING finger protein Siah‐1 as a protein interacting specifically with OBF‐1. This interaction is mediated by the C‐terminal part of Siah‐1 and by residues in the N‐terminus of OBF‐1, partly distinct from the residues required for formation of a complex with the Oct POU domains and the DNA. Interaction between Siah‐1 and OBF‐1 leads to downregulation of OBF‐1 protein level but not mRNA, and to a corresponding reduction in octamer site‐dependent transcription activation. Inhibition of the ubiquitin‐proteasome pathway in B cells leads to elevated levels of OBF‐1 protein. Furthermore, in immunized mice, OBF‐1 protein amounts are dramatically increased in primary activated B cells, without concomitant increase in OBF‐1 mRNA. These data suggest that Siah‐1 is part of a novel regulatory loop controlling the level of OBF‐1 protein in B cells.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.15.4143</identifier><identifier>PMID: 11483517</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; B cell transcription ; B-Lymphocytes - cytology ; B-Lymphocytes - metabolism ; Binding Sites ; Boronic Acids - pharmacology ; Cell Line ; Cell Line, Transformed ; Cysteine Endopeptidases ; Cysteine Proteinase Inhibitors - pharmacology ; Deoxyribonucleic acid ; DNA ; Down-Regulation ; Humans ; Immune response ; Immunization ; Mice ; Molecular Sequence Data ; Multienzyme Complexes ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; OBF-1 ; OBF-1 protein ; Proteasome Endopeptidase Complex ; RING finger proteins ; RNA Processing, Post-Transcriptional ; Siah-1 protein ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Transcriptional Activation ; ubiquitin-proteasome pathway ; Ubiquitin-Protein Ligases ; Ubiquitins - metabolism ; Up-Regulation ; Zinc Fingers</subject><ispartof>The EMBO journal, 2001-08, Vol.20 (15), p.4143-4152</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Aug 01, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6451-30a47ca96bff19ffaec35d38a840e6d8f36d25a1e136169b192c0003934a14bf3</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/PMC149178/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC149178/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11483517$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tiedt, Ralph</creatorcontrib><creatorcontrib>Bartholdy, Boris A.</creatorcontrib><creatorcontrib>Matthias, Gabriele</creatorcontrib><creatorcontrib>Newell, John W.</creatorcontrib><creatorcontrib>Matthias, Patrick</creatorcontrib><title>The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The transcriptional coactivator OBF‐1, which interacts with Oct‐1 and Oct‐2 and the octamer site DNA, has been shown to be critical for development of a normal immune response and the formation of germinal centers in secondary lymphoid organs. Here we have identified the RING finger protein Siah‐1 as a protein interacting specifically with OBF‐1. This interaction is mediated by the C‐terminal part of Siah‐1 and by residues in the N‐terminus of OBF‐1, partly distinct from the residues required for formation of a complex with the Oct POU domains and the DNA. Interaction between Siah‐1 and OBF‐1 leads to downregulation of OBF‐1 protein level but not mRNA, and to a corresponding reduction in octamer site‐dependent transcription activation. Inhibition of the ubiquitin‐proteasome pathway in B cells leads to elevated levels of OBF‐1 protein. Furthermore, in immunized mice, OBF‐1 protein amounts are dramatically increased in primary activated B cells, without concomitant increase in OBF‐1 mRNA. These data suggest that Siah‐1 is part of a novel regulatory loop controlling the level of OBF‐1 protein in B cells.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>B cell transcription</subject><subject>B-Lymphocytes - cytology</subject><subject>B-Lymphocytes - metabolism</subject><subject>Binding Sites</subject><subject>Boronic Acids - pharmacology</subject><subject>Cell Line</subject><subject>Cell Line, Transformed</subject><subject>Cysteine Endopeptidases</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Down-Regulation</subject><subject>Humans</subject><subject>Immune response</subject><subject>Immunization</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Multienzyme Complexes</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>OBF-1</subject><subject>OBF-1 protein</subject><subject>Proteasome Endopeptidase Complex</subject><subject>RING finger proteins</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>Siah-1 protein</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><subject>Transcriptional Activation</subject><subject>ubiquitin-proteasome pathway</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitins - metabolism</subject><subject>Up-Regulation</subject><subject>Zinc Fingers</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkk1vEzEQhi0EoqFw54RWHLht61l_rQ8caNWGltIKWoRUDpbXsROHzTrYm0D_PU43KgUJ9WSN_Dz2jF8j9BLwHmBJ9u2iCfP9KldsjwIlj9AIKMdlhQV7jEa44lBSqOUOepbSHGPMagFP0Q4ArQkDMULfrma2-HxyPi6c76Y2FssYeuu74tLrWQlFtNNVq3ubij6DrV3btgjutuij7pKJftn70Om2MEGb3q91H2JxcXBcwnP0xOk22RfbdRd9OT66Onxfnl2MTw7fnZWGUwYlwZoKoyVvnAPpnLaGsAmpdU2x5ZPaET6pmAYLhAOXDcjK5FGIJFQDbRzZRW-Hc5erZmEnxna5tVYto1_oeKOC9urvnc7P1DSsFVAJos7-m60fw4-VTb1a-GRs2-rOhlVSAjAHWeMHQRASC16RDL7-B5yHVcyPlBnJciqiZhnCA2RiSClad9cxYLWJV93Gq6pcMbWJNyuv7k_6R9jmmQE5AD99a28ePFAdfTw4FUwSCZBdGNyUtc1fuNf0_xsqB8en3v66u0_H74oLIpj6ej5Wny4_nPLra6Eo-Q2CZtJG</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Tiedt, Ralph</creator><creator>Bartholdy, Boris A.</creator><creator>Matthias, Gabriele</creator><creator>Newell, John W.</creator><creator>Matthias, Patrick</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Oxford University Press</general><scope>BSCLL</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>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>AEUYN</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>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>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010801</creationdate><title>The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1</title><author>Tiedt, Ralph ; Bartholdy, Boris A. ; Matthias, Gabriele ; Newell, John W. ; Matthias, Patrick</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6451-30a47ca96bff19ffaec35d38a840e6d8f36d25a1e136169b192c0003934a14bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>B cell transcription</topic><topic>B-Lymphocytes - 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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</fulltext></delivery><addata><au>Tiedt, Ralph</au><au>Bartholdy, Boris A.</au><au>Matthias, Gabriele</au><au>Newell, John W.</au><au>Matthias, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-08-01</date><risdate>2001</risdate><volume>20</volume><issue>15</issue><spage>4143</spage><epage>4152</epage><pages>4143-4152</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The transcriptional coactivator OBF‐1, which interacts with Oct‐1 and Oct‐2 and the octamer site DNA, has been shown to be critical for development of a normal immune response and the formation of germinal centers in secondary lymphoid organs. Here we have identified the RING finger protein Siah‐1 as a protein interacting specifically with OBF‐1. This interaction is mediated by the C‐terminal part of Siah‐1 and by residues in the N‐terminus of OBF‐1, partly distinct from the residues required for formation of a complex with the Oct POU domains and the DNA. Interaction between Siah‐1 and OBF‐1 leads to downregulation of OBF‐1 protein level but not mRNA, and to a corresponding reduction in octamer site‐dependent transcription activation. Inhibition of the ubiquitin‐proteasome pathway in B cells leads to elevated levels of OBF‐1 protein. Furthermore, in immunized mice, OBF‐1 protein amounts are dramatically increased in primary activated B cells, without concomitant increase in OBF‐1 mRNA. These data suggest that Siah‐1 is part of a novel regulatory loop controlling the level of OBF‐1 protein in B cells.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11483517</pmid><doi>10.1093/emboj/20.15.4143</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals B cell transcription B-Lymphocytes - cytology B-Lymphocytes - metabolism Binding Sites Boronic Acids - pharmacology Cell Line Cell Line, Transformed Cysteine Endopeptidases Cysteine Proteinase Inhibitors - pharmacology Deoxyribonucleic acid DNA Down-Regulation Humans Immune response Immunization Mice Molecular Sequence Data Multienzyme Complexes Nuclear Proteins - genetics Nuclear Proteins - metabolism OBF-1 OBF-1 protein Proteasome Endopeptidase Complex RING finger proteins RNA Processing, Post-Transcriptional Siah-1 protein Trans-Activators - genetics Trans-Activators - metabolism Transcriptional Activation ubiquitin-proteasome pathway Ubiquitin-Protein Ligases Ubiquitins - metabolism Up-Regulation Zinc Fingers |
| title | The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1 |
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