Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway
Transcriptional repression by nuclear hormone receptors is thought to result from a unison of targeting chromatin modification and disabling the basal transcriptional machinery. We used Xenopus oocytes to compare silencing effected by the thyroid hormone receptor (TR) and its mutated version, the on...
Gespeichert in:
Veröffentlicht in: | The EMBO journal 2000-08, Vol.19 (15), p.4074-4090 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 4090 |
---|---|
container_issue | 15 |
container_start_page | 4074 |
container_title | The EMBO journal |
container_volume | 19 |
creator | Urnov, Fyodor D. Yee, Janet Sachs, Laurent Collingwood, Trevor N. Bauer, Anton Beug, Hartmut Shi, Yun-Bo Wolffe, Alan P. |
description | Transcriptional repression by nuclear hormone receptors is thought to result from a unison of targeting chromatin modification and disabling the basal transcriptional machinery. We used
Xenopus
oocytes to compare silencing effected by the thyroid hormone receptor (TR) and its mutated version, the oncoprotein v‐ErbA, on partly and fully chromatinized TR‐responsive templates
in vivo
. Repression by v‐ErbA was not as efficient as that mediated by TR, was significantly more sensitive to histone deacetylase (HDAC) inhibitor treatment and, unlike TR, v‐ErbA required mature chromatin to effect repression. We find that both v‐ErbA and TR can recruit the corepressor N‐CoR, but, in contrast to existing models, show a concomitant enrichment for HDAC3 that occurs without an association with Sin3, HDAC1/RPD3, Mi‐2 or HDAC5. We propose a requirement for chromatin infrastructure in N‐CoR/HDAC3‐effected repression and suggest that the inability of v‐ErbA to silence on partly chromatinized templates may stem from its impaired capacity to interfere with basal transcriptional machinery function. In support of this notion, we find v‐ErbA to be less competent than TR for binding to TFIIB
in vitro
and
in vivo
. |
doi_str_mv | 10.1093/emboj/19.15.4074 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_306612</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>374518451</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6014-f27b0f10929c9e7ac6978ab88af9487298a8e10810ce0d7afbc6c4c2c3e6913a3</originalsourceid><addsrcrecordid>eNqFks1u1DAUhSMEokNhzwZksWCXqe382F6wKKOhgKalRUUsLce5mcmQsYOdtORBeF8cUg0DEurKsu75js-1ThQ9J3hOsEhOYFfY7QkRc5LNU8zSB9GMpDmOKWbZw2iGaU7ilHBxFD3xfosxzjgjj6OjAFPCOZ9FP6-VW0NXmzWyFbqIF_YzUqZEm9p31gAqQWnohkZ5QAkqBtRtAFmjbetsB7VBN_HSFadoqKEpPVJIb5zdqWCIalM55TvX6653EJfQginBdKhzynjt6rarrVENctA68D5cUKu6za0ankaPKtV4eHZ3Hkdf3i2vF-_j1aezD4vTVaxzTNK4oqzA1biM0AKY0rlgXBWcq0qknFHBFQeCOcEacMlUVehcp5rqBHJBEpUcR28m37YvdlDqkM6pRrau3ik3SKtq-ffE1Bu5tjcywXlOaOBf3_HOfu_Bd3JXew1NowzY3ktGaHgoY_cKCcsTRlMehK_-EW5t78IvBY3IaI5zOrrhSaSd9d5BtU9MsByLIX8XIxCSZHIsRkBeHm56AExNCAIxCW7rBoZ7DeXy_O1HlomE0tGcTKwPmFmDOwj9_0AvJsaosR77B_94xtM8FBF-7MfKfZM5S1gmv16cSXGZXNHV5ZU8T34BclDz-w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>195260627</pqid></control><display><type>article</type><title>Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway</title><source>Wiley-Blackwell Journals</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Open Access</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Urnov, Fyodor D. ; Yee, Janet ; Sachs, Laurent ; Collingwood, Trevor N. ; Bauer, Anton ; Beug, Hartmut ; Shi, Yun-Bo ; Wolffe, Alan P.</creator><creatorcontrib>Urnov, Fyodor D. ; Yee, Janet ; Sachs, Laurent ; Collingwood, Trevor N. ; Bauer, Anton ; Beug, Hartmut ; Shi, Yun-Bo ; Wolffe, Alan P.</creatorcontrib><description>Transcriptional repression by nuclear hormone receptors is thought to result from a unison of targeting chromatin modification and disabling the basal transcriptional machinery. We used
Xenopus
oocytes to compare silencing effected by the thyroid hormone receptor (TR) and its mutated version, the oncoprotein v‐ErbA, on partly and fully chromatinized TR‐responsive templates
in vivo
. Repression by v‐ErbA was not as efficient as that mediated by TR, was significantly more sensitive to histone deacetylase (HDAC) inhibitor treatment and, unlike TR, v‐ErbA required mature chromatin to effect repression. We find that both v‐ErbA and TR can recruit the corepressor N‐CoR, but, in contrast to existing models, show a concomitant enrichment for HDAC3 that occurs without an association with Sin3, HDAC1/RPD3, Mi‐2 or HDAC5. We propose a requirement for chromatin infrastructure in N‐CoR/HDAC3‐effected repression and suggest that the inability of v‐ErbA to silence on partly chromatinized templates may stem from its impaired capacity to interfere with basal transcriptional machinery function. In support of this notion, we find v‐ErbA to be less competent than TR for binding to TFIIB
in vitro
and
in vivo
.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/19.15.4074</identifier><identifier>PMID: 10921888</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adenosine Triphosphatases ; Animals ; Autoantigens - metabolism ; Chickens ; Chromatin - metabolism ; DNA Helicases ; Gene Expression Regulation ; histone deacetylase ; histone deacetylase (HDAC)3 ; Histone Deacetylase 1 ; Histone Deacetylases - metabolism ; Infrastructure ; Mi-2 Nucleosome Remodeling and Deacetylase Complex ; N-CoR ; N-CoR protein ; Nuclear Proteins - metabolism ; Nuclear Receptor Co-Repressor 1 ; Oncogene Proteins v-erbA - metabolism ; Oocytes ; Protein Binding ; Receptors, Thyroid Hormone - genetics ; Repressor Proteins - metabolism ; Saccharomyces cerevisiae Proteins ; Thyroid ; thyroid hormone receptor ; Transcription Factors - metabolism ; transcription initiation factor TFIIB ; Transcription, Genetic ; transcriptional repression ; v-ErbA ; v-ErbA protein ; Xenopus ; Xenopus laevis</subject><ispartof>The EMBO journal, 2000-08, Vol.19 (15), p.4074-4090</ispartof><rights>European Molecular Biology Organization 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Aug 01, 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6014-f27b0f10929c9e7ac6978ab88af9487298a8e10810ce0d7afbc6c4c2c3e6913a3</citedby><cites>FETCH-LOGICAL-c6014-f27b0f10929c9e7ac6978ab88af9487298a8e10810ce0d7afbc6c4c2c3e6913a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC306612/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC306612/$$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/10921888$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Urnov, Fyodor D.</creatorcontrib><creatorcontrib>Yee, Janet</creatorcontrib><creatorcontrib>Sachs, Laurent</creatorcontrib><creatorcontrib>Collingwood, Trevor N.</creatorcontrib><creatorcontrib>Bauer, Anton</creatorcontrib><creatorcontrib>Beug, Hartmut</creatorcontrib><creatorcontrib>Shi, Yun-Bo</creatorcontrib><creatorcontrib>Wolffe, Alan P.</creatorcontrib><title>Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Transcriptional repression by nuclear hormone receptors is thought to result from a unison of targeting chromatin modification and disabling the basal transcriptional machinery. We used
Xenopus
oocytes to compare silencing effected by the thyroid hormone receptor (TR) and its mutated version, the oncoprotein v‐ErbA, on partly and fully chromatinized TR‐responsive templates
in vivo
. Repression by v‐ErbA was not as efficient as that mediated by TR, was significantly more sensitive to histone deacetylase (HDAC) inhibitor treatment and, unlike TR, v‐ErbA required mature chromatin to effect repression. We find that both v‐ErbA and TR can recruit the corepressor N‐CoR, but, in contrast to existing models, show a concomitant enrichment for HDAC3 that occurs without an association with Sin3, HDAC1/RPD3, Mi‐2 or HDAC5. We propose a requirement for chromatin infrastructure in N‐CoR/HDAC3‐effected repression and suggest that the inability of v‐ErbA to silence on partly chromatinized templates may stem from its impaired capacity to interfere with basal transcriptional machinery function. In support of this notion, we find v‐ErbA to be less competent than TR for binding to TFIIB
in vitro
and
in vivo
.</description><subject>Adenosine Triphosphatases</subject><subject>Animals</subject><subject>Autoantigens - metabolism</subject><subject>Chickens</subject><subject>Chromatin - metabolism</subject><subject>DNA Helicases</subject><subject>Gene Expression Regulation</subject><subject>histone deacetylase</subject><subject>histone deacetylase (HDAC)3</subject><subject>Histone Deacetylase 1</subject><subject>Histone Deacetylases - metabolism</subject><subject>Infrastructure</subject><subject>Mi-2 Nucleosome Remodeling and Deacetylase Complex</subject><subject>N-CoR</subject><subject>N-CoR protein</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nuclear Receptor Co-Repressor 1</subject><subject>Oncogene Proteins v-erbA - metabolism</subject><subject>Oocytes</subject><subject>Protein Binding</subject><subject>Receptors, Thyroid Hormone - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Thyroid</subject><subject>thyroid hormone receptor</subject><subject>Transcription Factors - metabolism</subject><subject>transcription initiation factor TFIIB</subject><subject>Transcription, Genetic</subject><subject>transcriptional repression</subject><subject>v-ErbA</subject><subject>v-ErbA protein</subject><subject>Xenopus</subject><subject>Xenopus laevis</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</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>eNqFks1u1DAUhSMEokNhzwZksWCXqe382F6wKKOhgKalRUUsLce5mcmQsYOdtORBeF8cUg0DEurKsu75js-1ThQ9J3hOsEhOYFfY7QkRc5LNU8zSB9GMpDmOKWbZw2iGaU7ilHBxFD3xfosxzjgjj6OjAFPCOZ9FP6-VW0NXmzWyFbqIF_YzUqZEm9p31gAqQWnohkZ5QAkqBtRtAFmjbetsB7VBN_HSFadoqKEpPVJIb5zdqWCIalM55TvX6653EJfQginBdKhzynjt6rarrVENctA68D5cUKu6za0ankaPKtV4eHZ3Hkdf3i2vF-_j1aezD4vTVaxzTNK4oqzA1biM0AKY0rlgXBWcq0qknFHBFQeCOcEacMlUVehcp5rqBHJBEpUcR28m37YvdlDqkM6pRrau3ik3SKtq-ffE1Bu5tjcywXlOaOBf3_HOfu_Bd3JXew1NowzY3ktGaHgoY_cKCcsTRlMehK_-EW5t78IvBY3IaI5zOrrhSaSd9d5BtU9MsByLIX8XIxCSZHIsRkBeHm56AExNCAIxCW7rBoZ7DeXy_O1HlomE0tGcTKwPmFmDOwj9_0AvJsaosR77B_94xtM8FBF-7MfKfZM5S1gmv16cSXGZXNHV5ZU8T34BclDz-w</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Urnov, Fyodor D.</creator><creator>Yee, Janet</creator><creator>Sachs, Laurent</creator><creator>Collingwood, Trevor N.</creator><creator>Bauer, Anton</creator><creator>Beug, Hartmut</creator><creator>Shi, Yun-Bo</creator><creator>Wolffe, Alan P.</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>20000801</creationdate><title>Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway</title><author>Urnov, Fyodor D. ; Yee, Janet ; Sachs, Laurent ; Collingwood, Trevor N. ; Bauer, Anton ; Beug, Hartmut ; Shi, Yun-Bo ; Wolffe, Alan P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6014-f27b0f10929c9e7ac6978ab88af9487298a8e10810ce0d7afbc6c4c2c3e6913a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adenosine Triphosphatases</topic><topic>Animals</topic><topic>Autoantigens - metabolism</topic><topic>Chickens</topic><topic>Chromatin - metabolism</topic><topic>DNA Helicases</topic><topic>Gene Expression Regulation</topic><topic>histone deacetylase</topic><topic>histone deacetylase (HDAC)3</topic><topic>Histone Deacetylase 1</topic><topic>Histone Deacetylases - metabolism</topic><topic>Infrastructure</topic><topic>Mi-2 Nucleosome Remodeling and Deacetylase Complex</topic><topic>N-CoR</topic><topic>N-CoR protein</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nuclear Receptor Co-Repressor 1</topic><topic>Oncogene Proteins v-erbA - metabolism</topic><topic>Oocytes</topic><topic>Protein Binding</topic><topic>Receptors, Thyroid Hormone - genetics</topic><topic>Repressor Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Thyroid</topic><topic>thyroid hormone receptor</topic><topic>Transcription Factors - metabolism</topic><topic>transcription initiation factor TFIIB</topic><topic>Transcription, Genetic</topic><topic>transcriptional repression</topic><topic>v-ErbA</topic><topic>v-ErbA protein</topic><topic>Xenopus</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Urnov, Fyodor D.</creatorcontrib><creatorcontrib>Yee, Janet</creatorcontrib><creatorcontrib>Sachs, Laurent</creatorcontrib><creatorcontrib>Collingwood, Trevor N.</creatorcontrib><creatorcontrib>Bauer, Anton</creatorcontrib><creatorcontrib>Beug, Hartmut</creatorcontrib><creatorcontrib>Shi, Yun-Bo</creatorcontrib><creatorcontrib>Wolffe, Alan P.</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>ProQuest Health and Medical</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 (Proquest)</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)</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>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest_Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</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>Urnov, Fyodor D.</au><au>Yee, Janet</au><au>Sachs, Laurent</au><au>Collingwood, Trevor N.</au><au>Bauer, Anton</au><au>Beug, Hartmut</au><au>Shi, Yun-Bo</au><au>Wolffe, Alan P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>19</volume><issue>15</issue><spage>4074</spage><epage>4090</epage><pages>4074-4090</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Transcriptional repression by nuclear hormone receptors is thought to result from a unison of targeting chromatin modification and disabling the basal transcriptional machinery. We used
Xenopus
oocytes to compare silencing effected by the thyroid hormone receptor (TR) and its mutated version, the oncoprotein v‐ErbA, on partly and fully chromatinized TR‐responsive templates
in vivo
. Repression by v‐ErbA was not as efficient as that mediated by TR, was significantly more sensitive to histone deacetylase (HDAC) inhibitor treatment and, unlike TR, v‐ErbA required mature chromatin to effect repression. We find that both v‐ErbA and TR can recruit the corepressor N‐CoR, but, in contrast to existing models, show a concomitant enrichment for HDAC3 that occurs without an association with Sin3, HDAC1/RPD3, Mi‐2 or HDAC5. We propose a requirement for chromatin infrastructure in N‐CoR/HDAC3‐effected repression and suggest that the inability of v‐ErbA to silence on partly chromatinized templates may stem from its impaired capacity to interfere with basal transcriptional machinery function. In support of this notion, we find v‐ErbA to be less competent than TR for binding to TFIIB
in vitro
and
in vivo
.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>10921888</pmid><doi>10.1093/emboj/19.15.4074</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0261-4189 |
ispartof | The EMBO journal, 2000-08, Vol.19 (15), p.4074-4090 |
issn | 0261-4189 1460-2075 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_306612 |
source | Wiley-Blackwell Journals; MEDLINE; EZB-FREE-00999 freely available EZB journals; Wiley Open Access; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Adenosine Triphosphatases Animals Autoantigens - metabolism Chickens Chromatin - metabolism DNA Helicases Gene Expression Regulation histone deacetylase histone deacetylase (HDAC)3 Histone Deacetylase 1 Histone Deacetylases - metabolism Infrastructure Mi-2 Nucleosome Remodeling and Deacetylase Complex N-CoR N-CoR protein Nuclear Proteins - metabolism Nuclear Receptor Co-Repressor 1 Oncogene Proteins v-erbA - metabolism Oocytes Protein Binding Receptors, Thyroid Hormone - genetics Repressor Proteins - metabolism Saccharomyces cerevisiae Proteins Thyroid thyroid hormone receptor Transcription Factors - metabolism transcription initiation factor TFIIB Transcription, Genetic transcriptional repression v-ErbA v-ErbA protein Xenopus Xenopus laevis |
title | Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-ErbA yields a chromatin infrastructure-dependent transcriptional repression pathway |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T06%3A26%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Targeting%20of%20N-CoR%20and%20histone%20deacetylase%203%20by%20the%20oncoprotein%20v-ErbA%20yields%20a%20chromatin%20infrastructure-dependent%20transcriptional%20repression%20pathway&rft.jtitle=The%20EMBO%20journal&rft.au=Urnov,%20Fyodor%20D.&rft.date=2000-08-01&rft.volume=19&rft.issue=15&rft.spage=4074&rft.epage=4090&rft.pages=4074-4090&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1093/emboj/19.15.4074&rft_dat=%3Cproquest_pubme%3E374518451%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=195260627&rft_id=info:pmid/10921888&rfr_iscdi=true |