Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1
The Brf1 subunit of TFIIIB plays an important role in recruiting the TATA-binding protein (TBP) to the up-stream region of genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through dimerization. Promoter assembly factors therefore might...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-07, Vol.279 (31), p.32401-32406 |
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| container_issue | 31 |
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| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Alexander, Diane E Kaczorowski, David J Jackson-Fisher, Amy J Lowery, Drew M Zanton, Sara J Pugh, B Franklin |
| description | The Brf1 subunit of TFIIIB plays an important role in recruiting the TATA-binding protein (TBP) to the up-stream region of
genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through
dimerization. Promoter assembly factors therefore might be required to dissociate TBP into productively binding monomers.
Here we show that Saccharomyces cerevisiae Brf1 induces TBP dimers to dissociate. The high affinity TBP binding domain of Brf1 is not sufficient to promote TBP dimer
dissociation but in addition requires the TFIIB homology domain of Brf1. A model is proposed to explain how two distinct functional
domains of Brf1 work in concert to dissociate TBP into monomers. |
| doi_str_mv | 10.1074/jbc.M405782200 |
| format | Article |
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genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through
dimerization. Promoter assembly factors therefore might be required to dissociate TBP into productively binding monomers.
Here we show that Saccharomyces cerevisiae Brf1 induces TBP dimers to dissociate. The high affinity TBP binding domain of Brf1 is not sufficient to promote TBP dimer
dissociation but in addition requires the TFIIB homology domain of Brf1. A model is proposed to explain how two distinct functional
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genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through
dimerization. Promoter assembly factors therefore might be required to dissociate TBP into productively binding monomers.
Here we show that Saccharomyces cerevisiae Brf1 induces TBP dimers to dissociate. The high affinity TBP binding domain of Brf1 is not sufficient to promote TBP dimer
dissociation but in addition requires the TFIIB homology domain of Brf1. A model is proposed to explain how two distinct functional
domains of Brf1 work in concert to dissociate TBP into monomers.</description><subject>Alleles</subject><subject>Cross-Linking Reagents - pharmacology</subject><subject>Dimerization</subject><subject>Gene Deletion</subject><subject>Glutathione Transferase - metabolism</subject><subject>Humans</subject><subject>Models, Biological</subject><subject>Mutation</subject><subject>Plasmids - metabolism</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA Polymerase III - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>TATA-Binding Protein Associated Factors</subject><subject>TATA-Box Binding Protein - chemistry</subject><subject>Time Factors</subject><subject>Transcription Factor TFIIIB - chemistry</subject><subject>Transcription Factor TFIIIB - metabolism</subject><subject>Transcription, Genetic</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpF0MtLAzEQBvAgitbH1aPkIN62Th7bTY61vhZ8IRW8hSSbtSndTU22SP3rXW3BuQwMv_kOH0KnBIYECn45N3b4yCEvBKUAO2hAQLCM5eR9Fw0AKMkkzcUBOkxpDv1wSfbRAcmJBBixAZqX7cwb3_nQ4lDj6Xg6xle-rXz7gV9i6Jxv8bVvXPTf-g-ZNX59GuOXsFj3V50cLssST6Nuk41--WfKtg_c8FttuxDxVazJMdqr9SK5k-0-Qm-3N9PJffbwfFdOxg-ZZZJ0mdQF5ZYJxxkrWMV0zZiQBVieC1NJI8xIguEV5aPaapCCcMdHBc9ZXRXEWXaELja5yxg-Vy51qvHJusVCty6skiICaP8kezjcQBtDStHVahl9o-NaEVC_7aq-XfXfbv9wtk1emcZV_3xbZw_ON2DmP2ZfPjplfLAz1yhaSMWIYpQDYT9jwoCQ</recordid><startdate>20040730</startdate><enddate>20040730</enddate><creator>Alexander, Diane E</creator><creator>Kaczorowski, David J</creator><creator>Jackson-Fisher, Amy J</creator><creator>Lowery, Drew M</creator><creator>Zanton, Sara J</creator><creator>Pugh, B Franklin</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>M7N</scope></search><sort><creationdate>20040730</creationdate><title>Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1</title><author>Alexander, Diane E ; Kaczorowski, David J ; Jackson-Fisher, Amy J ; Lowery, Drew M ; Zanton, Sara J ; Pugh, B Franklin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-9a724c38e43373d3af338970c458bd9b8b690b4d246fca09814e467453fd71ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Alleles</topic><topic>Cross-Linking Reagents - pharmacology</topic><topic>Dimerization</topic><topic>Gene Deletion</topic><topic>Glutathione Transferase - metabolism</topic><topic>Humans</topic><topic>Models, Biological</topic><topic>Mutation</topic><topic>Plasmids - metabolism</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA Polymerase III - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>TATA-Binding Protein Associated Factors</topic><topic>TATA-Box Binding Protein - chemistry</topic><topic>Time Factors</topic><topic>Transcription Factor TFIIIB - chemistry</topic><topic>Transcription Factor TFIIIB - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alexander, Diane E</creatorcontrib><creatorcontrib>Kaczorowski, David J</creatorcontrib><creatorcontrib>Jackson-Fisher, Amy J</creatorcontrib><creatorcontrib>Lowery, Drew M</creatorcontrib><creatorcontrib>Zanton, Sara J</creatorcontrib><creatorcontrib>Pugh, B Franklin</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alexander, Diane E</au><au>Kaczorowski, David J</au><au>Jackson-Fisher, Amy J</au><au>Lowery, Drew M</au><au>Zanton, Sara J</au><au>Pugh, B Franklin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-07-30</date><risdate>2004</risdate><volume>279</volume><issue>31</issue><spage>32401</spage><epage>32406</epage><pages>32401-32406</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The Brf1 subunit of TFIIIB plays an important role in recruiting the TATA-binding protein (TBP) to the up-stream region of
genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through
dimerization. Promoter assembly factors therefore might be required to dissociate TBP into productively binding monomers.
Here we show that Saccharomyces cerevisiae Brf1 induces TBP dimers to dissociate. The high affinity TBP binding domain of Brf1 is not sufficient to promote TBP dimer
dissociation but in addition requires the TFIIB homology domain of Brf1. A model is proposed to explain how two distinct functional
domains of Brf1 work in concert to dissociate TBP into monomers.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15190063</pmid><doi>10.1074/jbc.M405782200</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32401-32406 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alleles Cross-Linking Reagents - pharmacology Dimerization Gene Deletion Glutathione Transferase - metabolism Humans Models, Biological Mutation Plasmids - metabolism Promoter Regions, Genetic Protein Binding Protein Structure, Tertiary Recombinant Proteins - chemistry Reverse Transcriptase Polymerase Chain Reaction RNA Polymerase III - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins TATA-Binding Protein Associated Factors TATA-Box Binding Protein - chemistry Time Factors Transcription Factor TFIIIB - chemistry Transcription Factor TFIIIB - metabolism Transcription, Genetic |
| title | Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1 |
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