Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1
Corepressors N‐CoR and SMRT participate in diverse repression pathways and exist in large protein complexes including HDAC3, TBL1 and TBLR1. However, the roles of these proteins in SMRT–N‐CoR complex function are largely unknown. Here we report the purification and functional characterization of the...
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| Veröffentlicht in: | The EMBO journal 2003-03, Vol.22 (6), p.1336-1346 |
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| creator | Yoon, Ho-Geun Chan, Doug W. Huang, Zhi-Qing Li, Jiwen Fondell, Joseph D. Qin, Jun Wong, Jiemin |
| description | Corepressors N‐CoR and SMRT participate in diverse repression pathways and exist in large protein complexes including HDAC3, TBL1 and TBLR1. However, the roles of these proteins in SMRT–N‐CoR complex function are largely unknown. Here we report the purification and functional characterization of the human N‐CoR complex. The purified N‐CoR complex contains 10–12 associated proteins, including previously identified components and a novel actin‐binding protein IR10. We show that TBL1/TBLR1 associates with N‐CoR through two independent interactions: the N‐terminal region and the C‐terminal WD‐40 repeats interact with the N‐CoR RD1 and RD4 region, respectively.
In vitro
, TBL1/TBLR1 bind histones H2B and H4, and, importantly, repression by TBL1/TBLR1 correlates with their interaction with histones. By using specific small interference RNAs (siRNAs), we demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor. Together, our data reveal the roles of HDAC3 and TBL/TBLR1 and provide evidence for the functional importance of histone interaction in repression mediated by SMRT–N‐CoR complexes. |
| doi_str_mv | 10.1093/emboj/cdg120 |
| format | Article |
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In vitro
, TBL1/TBLR1 bind histones H2B and H4, and, importantly, repression by TBL1/TBLR1 correlates with their interaction with histones. By using specific small interference RNAs (siRNAs), we demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor. Together, our data reveal the roles of HDAC3 and TBL/TBLR1 and provide evidence for the functional importance of histone interaction in repression mediated by SMRT–N‐CoR complexes.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/cdg120</identifier><identifier>PMID: 12628926</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Cell Line ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - isolation & purification ; EMBO09 ; HDAC3 ; HeLa Cells ; Histone Deacetylases - chemistry ; Histone Deacetylases - metabolism ; histone interaction ; Histones - metabolism ; Humans ; Microfilament Proteins - chemistry ; N-CoR ; Nuclear Proteins - chemistry ; Nuclear Proteins - isolation & purification ; Nuclear Proteins - metabolism ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits ; Receptors, Cytoplasmic and Nuclear ; Receptors, Thyroid Hormone - metabolism ; Recombinant Proteins - metabolism ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - isolation & purification ; Repressor Proteins - metabolism ; RNA, Small Interfering - metabolism ; Sequence Homology, Amino Acid ; TBL1 ; TBLR1 ; Thyroid ; Transducin - chemistry ; Transducin - metabolism</subject><ispartof>The EMBO journal, 2003-03, Vol.22 (6), p.1336-1346</ispartof><rights>European Molecular Biology Organization 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Mar 17, 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6472-d99b988d2b9c959bf07287b592b0ee0bd34e3df9bc0332d6d6cc423648418b4c3</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/PMC151047/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC151047/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12628926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoon, Ho-Geun</creatorcontrib><creatorcontrib>Chan, Doug W.</creatorcontrib><creatorcontrib>Huang, Zhi-Qing</creatorcontrib><creatorcontrib>Li, Jiwen</creatorcontrib><creatorcontrib>Fondell, Joseph D.</creatorcontrib><creatorcontrib>Qin, Jun</creatorcontrib><creatorcontrib>Wong, Jiemin</creatorcontrib><title>Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Corepressors N‐CoR and SMRT participate in diverse repression pathways and exist in large protein complexes including HDAC3, TBL1 and TBLR1. However, the roles of these proteins in SMRT–N‐CoR complex function are largely unknown. Here we report the purification and functional characterization of the human N‐CoR complex. The purified N‐CoR complex contains 10–12 associated proteins, including previously identified components and a novel actin‐binding protein IR10. We show that TBL1/TBLR1 associates with N‐CoR through two independent interactions: the N‐terminal region and the C‐terminal WD‐40 repeats interact with the N‐CoR RD1 and RD4 region, respectively.
In vitro
, TBL1/TBLR1 bind histones H2B and H4, and, importantly, repression by TBL1/TBLR1 correlates with their interaction with histones. By using specific small interference RNAs (siRNAs), we demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor. Together, our data reveal the roles of HDAC3 and TBL/TBLR1 and provide evidence for the functional importance of histone interaction in repression mediated by SMRT–N‐CoR complexes.</description><subject>Amino Acid Sequence</subject><subject>Cell Line</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>EMBO09</subject><subject>HDAC3</subject><subject>HeLa Cells</subject><subject>Histone Deacetylases - chemistry</subject><subject>Histone Deacetylases - metabolism</subject><subject>histone interaction</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Microfilament Proteins - chemistry</subject><subject>N-CoR</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Nuclear Proteins - metabolism</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits</subject><subject>Receptors, Cytoplasmic and Nuclear</subject><subject>Receptors, Thyroid Hormone - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - isolation & purification</subject><subject>Repressor Proteins - metabolism</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>TBL1</subject><subject>TBLR1</subject><subject>Thyroid</subject><subject>Transducin - chemistry</subject><subject>Transducin - metabolism</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</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>eNqFkc9v0zAcxS0EYmVw4wqKOHBamH_EdjyJw1ZGC3QDTUNIXCzHcVp3SVzsBDb-etymKuOH4GRb7_Oen_0F4DGCLxAU5NA0hVse6nKOMLwDRihjMMWQ07tgBDFDaYZysQcehLCEENKco_tgD2GGc4HZCFx96L2trFaddW2i2jKp-lavD6pO9EJ5pTvj7fdBd1XSLUyy6BvVJufp2F0k2jWr2lwfbQTvahPW1PTV8ZgcJJcnM7QJjZsL9BDcq1QdzKPtug8-vj69HE_T2fvJm_HxLNUs4zgthShEnpe4EFpQUVSQ45wXVOACGgOLkmSGlJUoNCQEl6xkWmeYsCyPTy0yTfbByyF31ReNKbVpO69qufK2Uf5GOmXlr0prF3LuvkpEEcx49D_f-r370pvQycYGbepatcb1QXICORc4_y-Ick6wYDiCz34Dl6738YsjIyimHDMWoYMB0t6F4E21a4ygXI9abkYth1FH_OntV_6Et7ONAB2Ab7Y2N_8Mk6dnJ285FRSSddl08IVoaefG3yr79yJPBr5VXe_N7qI_8mzozPVOVv5KMk44lZ_OJ3IyfXcmGGLyM_kBFXnehQ</recordid><startdate>20030317</startdate><enddate>20030317</enddate><creator>Yoon, Ho-Geun</creator><creator>Chan, Doug W.</creator><creator>Huang, Zhi-Qing</creator><creator>Li, Jiwen</creator><creator>Fondell, Joseph D.</creator><creator>Qin, Jun</creator><creator>Wong, Jiemin</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</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>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>20030317</creationdate><title>Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1</title><author>Yoon, Ho-Geun ; Chan, Doug W. ; Huang, Zhi-Qing ; Li, Jiwen ; Fondell, Joseph D. ; Qin, Jun ; Wong, Jiemin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6472-d99b988d2b9c959bf07287b592b0ee0bd34e3df9bc0332d6d6cc423648418b4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Cell Line</topic><topic>DNA-Binding Proteins - 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isolation & purification</topic><topic>Repressor Proteins - metabolism</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>TBL1</topic><topic>TBLR1</topic><topic>Thyroid</topic><topic>Transducin - chemistry</topic><topic>Transducin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoon, Ho-Geun</creatorcontrib><creatorcontrib>Chan, Doug W.</creatorcontrib><creatorcontrib>Huang, Zhi-Qing</creatorcontrib><creatorcontrib>Li, Jiwen</creatorcontrib><creatorcontrib>Fondell, Joseph D.</creatorcontrib><creatorcontrib>Qin, Jun</creatorcontrib><creatorcontrib>Wong, Jiemin</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - 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>Yoon, Ho-Geun</au><au>Chan, Doug W.</au><au>Huang, Zhi-Qing</au><au>Li, Jiwen</au><au>Fondell, Joseph D.</au><au>Qin, Jun</au><au>Wong, Jiemin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2003-03-17</date><risdate>2003</risdate><volume>22</volume><issue>6</issue><spage>1336</spage><epage>1346</epage><pages>1336-1346</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Corepressors N‐CoR and SMRT participate in diverse repression pathways and exist in large protein complexes including HDAC3, TBL1 and TBLR1. However, the roles of these proteins in SMRT–N‐CoR complex function are largely unknown. Here we report the purification and functional characterization of the human N‐CoR complex. The purified N‐CoR complex contains 10–12 associated proteins, including previously identified components and a novel actin‐binding protein IR10. We show that TBL1/TBLR1 associates with N‐CoR through two independent interactions: the N‐terminal region and the C‐terminal WD‐40 repeats interact with the N‐CoR RD1 and RD4 region, respectively.
In vitro
, TBL1/TBLR1 bind histones H2B and H4, and, importantly, repression by TBL1/TBLR1 correlates with their interaction with histones. By using specific small interference RNAs (siRNAs), we demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor. Together, our data reveal the roles of HDAC3 and TBL/TBLR1 and provide evidence for the functional importance of histone interaction in repression mediated by SMRT–N‐CoR complexes.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12628926</pmid><doi>10.1093/emboj/cdg120</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Cell Line DNA-Binding Proteins - chemistry DNA-Binding Proteins - isolation & purification EMBO09 HDAC3 HeLa Cells Histone Deacetylases - chemistry Histone Deacetylases - metabolism histone interaction Histones - metabolism Humans Microfilament Proteins - chemistry N-CoR Nuclear Proteins - chemistry Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Peptide Fragments - chemistry Peptide Fragments - immunology Protein Binding Protein Structure, Tertiary Protein Subunits Receptors, Cytoplasmic and Nuclear Receptors, Thyroid Hormone - metabolism Recombinant Proteins - metabolism Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - isolation & purification Repressor Proteins - metabolism RNA, Small Interfering - metabolism Sequence Homology, Amino Acid TBL1 TBLR1 Thyroid Transducin - chemistry Transducin - metabolism |
| title | Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1 |
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