Use of a Genetically Introduced Cross-linker to Identify Interaction Sites of Acidic Activators within Native Transcription Factor IID and SAGA
An important goal is to identify the direct activation domain (AD)-interacting components of the transcriptional machinery within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator, and Swi/Snf coactivator complexes from transcriptional...
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| Veröffentlicht in: | The Journal of biological chemistry 2003-02, Vol.278 (9), p.6779-6786 |
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| container_issue | 9 |
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| container_title | The Journal of biological chemistry |
| container_volume | 278 |
| creator | Klein, Joachim Nolden, Mark Sanders, Steven L Kirchner, Jay Weil, P Anthony Melcher, Karsten |
| description | An important goal is to identify the direct activation domain (AD)-interacting components of the transcriptional machinery
within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator,
and Swi/Snf coactivator complexes from transcriptionally competent whole-cell yeast extracts were all capable of specifically
interacting with the prototypic acidic ADs of Gal4 and VP16. We then used hexahistidine tags as genetically introduced activation
domain-localized cross-linking receptors. In combination with immunological reagents against all subunits of TFIID and SAGA,
we systematically identified the direct AD-interacting subunits within the AD-TFIID and AD-SAGA coactivator complexes enriched
from whole-cell extracts and confirmed these results using purified TFIID and partially purified SAGA. Both ADs directly cross-linked
to TBP and to a subset of TFIID and SAGA subunits that carry histone-fold motifs. |
| doi_str_mv | 10.1074/jbc.M212514200 |
| format | Article |
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within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator,
and Swi/Snf coactivator complexes from transcriptionally competent whole-cell yeast extracts were all capable of specifically
interacting with the prototypic acidic ADs of Gal4 and VP16. We then used hexahistidine tags as genetically introduced activation
domain-localized cross-linking receptors. In combination with immunological reagents against all subunits of TFIID and SAGA,
we systematically identified the direct AD-interacting subunits within the AD-TFIID and AD-SAGA coactivator complexes enriched
from whole-cell extracts and confirmed these results using purified TFIID and partially purified SAGA. Both ADs directly cross-linked
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within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator,
and Swi/Snf coactivator complexes from transcriptionally competent whole-cell yeast extracts were all capable of specifically
interacting with the prototypic acidic ADs of Gal4 and VP16. We then used hexahistidine tags as genetically introduced activation
domain-localized cross-linking receptors. In combination with immunological reagents against all subunits of TFIID and SAGA,
we systematically identified the direct AD-interacting subunits within the AD-TFIID and AD-SAGA coactivator complexes enriched
from whole-cell extracts and confirmed these results using purified TFIID and partially purified SAGA. Both ADs directly cross-linked
to TBP and to a subset of TFIID and SAGA subunits that carry histone-fold motifs.</description><subject>Acetyltransferases - chemistry</subject><subject>Acetyltransferases - metabolism</subject><subject>Amino Acid Motifs</subject><subject>Binding Sites</subject><subject>Cross-Linking Reagents - pharmacology</subject><subject>Endopeptidases - metabolism</subject><subject>Histidine - chemistry</subject><subject>Histone Acetyltransferases</subject><subject>Histones</subject><subject>Models, Biological</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>TATA-Binding Protein Associated Factors - metabolism</subject><subject>Transcription Factor TFIID - chemistry</subject><subject>Transcription Factor TFIID - metabolism</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Yeasts</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS0EakPpliWyWLCb4MfYnllGgYaR-li0ldhZHvsOcZmMg-1Q9Vfwl3GaSF32bo509Z0j3XsQ-kjJnBJVf33o7fyKUSZozQh5g2aUNLzigv58i2aEMFq1TDSn6H1KD6RM3dITdFp4QlktZujffQIcBmzwCibI3ppxfMLdlGNwOwsOL2NIqRr99BsizgF3Dqbsh2cGorHZhwnf-gxpH7Ow3nlbJPu_JoeY8KPPaz_ha1M2gO-imZKNfvtsuyj2EHHXfcNmcvh2sVp8QO8GMyY4P-oZur_4frf8UV3erLrl4rKyvGlzJcvtwlhpGytbsExx20JfKy6pGoQStSLWSdYzoXo5NMqVwwUxrheKSgaGn6Evh9xtDH92kLLe-GRhHM0EYZe04oSThrJXQdpIRVirCjg_gHb_sQiD3ka_MfFJU6L3XenSlX7pqhg-HZN3_QbcC34spwCfD8Da_1o_-gi698GuYaOZanSrpVIt_w-o6ptD</recordid><startdate>20030228</startdate><enddate>20030228</enddate><creator>Klein, Joachim</creator><creator>Nolden, Mark</creator><creator>Sanders, Steven L</creator><creator>Kirchner, Jay</creator><creator>Weil, P Anthony</creator><creator>Melcher, Karsten</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20030228</creationdate><title>Use of a Genetically Introduced Cross-linker to Identify Interaction Sites of Acidic Activators within Native Transcription Factor IID and SAGA</title><author>Klein, Joachim ; Nolden, Mark ; Sanders, Steven L ; Kirchner, Jay ; Weil, P Anthony ; Melcher, Karsten</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-60745ac6c8c69ec273c9eb473617f575470cd62b257b6f87d04950adb57162ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetyltransferases - chemistry</topic><topic>Acetyltransferases - metabolism</topic><topic>Amino Acid Motifs</topic><topic>Binding Sites</topic><topic>Cross-Linking Reagents - pharmacology</topic><topic>Endopeptidases - metabolism</topic><topic>Histidine - chemistry</topic><topic>Histone Acetyltransferases</topic><topic>Histones</topic><topic>Models, Biological</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>TATA-Binding Protein Associated Factors - metabolism</topic><topic>Transcription Factor TFIID - chemistry</topic><topic>Transcription Factor TFIID - metabolism</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Klein, Joachim</creatorcontrib><creatorcontrib>Nolden, Mark</creatorcontrib><creatorcontrib>Sanders, Steven L</creatorcontrib><creatorcontrib>Kirchner, Jay</creatorcontrib><creatorcontrib>Weil, P Anthony</creatorcontrib><creatorcontrib>Melcher, Karsten</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Klein, Joachim</au><au>Nolden, Mark</au><au>Sanders, Steven L</au><au>Kirchner, Jay</au><au>Weil, P Anthony</au><au>Melcher, Karsten</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Use of a Genetically Introduced Cross-linker to Identify Interaction Sites of Acidic Activators within Native Transcription Factor IID and SAGA</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2003-02-28</date><risdate>2003</risdate><volume>278</volume><issue>9</issue><spage>6779</spage><epage>6786</epage><pages>6779-6786</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>An important goal is to identify the direct activation domain (AD)-interacting components of the transcriptional machinery
within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator,
and Swi/Snf coactivator complexes from transcriptionally competent whole-cell yeast extracts were all capable of specifically
interacting with the prototypic acidic ADs of Gal4 and VP16. We then used hexahistidine tags as genetically introduced activation
domain-localized cross-linking receptors. In combination with immunological reagents against all subunits of TFIID and SAGA,
we systematically identified the direct AD-interacting subunits within the AD-TFIID and AD-SAGA coactivator complexes enriched
from whole-cell extracts and confirmed these results using purified TFIID and partially purified SAGA. Both ADs directly cross-linked
to TBP and to a subset of TFIID and SAGA subunits that carry histone-fold motifs.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>12501245</pmid><doi>10.1074/jbc.M212514200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetyltransferases - chemistry Acetyltransferases - metabolism Amino Acid Motifs Binding Sites Cross-Linking Reagents - pharmacology Endopeptidases - metabolism Histidine - chemistry Histone Acetyltransferases Histones Models, Biological Protein Binding Protein Folding Protein Structure, Tertiary Recombinant Fusion Proteins - metabolism Recombinant Proteins - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism TATA-Binding Protein Associated Factors - metabolism Transcription Factor TFIID - chemistry Transcription Factor TFIID - metabolism Transcription Factors - metabolism Transcription, Genetic Yeasts |
| title | Use of a Genetically Introduced Cross-linker to Identify Interaction Sites of Acidic Activators within Native Transcription Factor IID and SAGA |
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