Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription
Dr1, a repressor of class II genes, regulates transcription by a novel mechanism. Biochemical analyses reveal that Dr1 directly interacts with the multiprotein TFIID complex. By use of the yeast two-hybrid system, we demonstrate that the association of Dr1 with the TATA-binding protein (TBP) subunit...
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| Veröffentlicht in: | Genes & development 1994-09, Vol.8 (17), p.2097-2109 |
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| container_end_page | 2109 |
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| container_issue | 17 |
| container_start_page | 2097 |
| container_title | Genes & development |
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| creator | Yeung, K C Inostroza, J A Mermelstein, F H Kannabiran, C Reinberg, D |
| description | Dr1, a repressor of class II genes, regulates transcription by a novel mechanism. Biochemical analyses reveal that Dr1 directly interacts with the multiprotein TFIID complex. By use of the yeast two-hybrid system, we demonstrate that the association of Dr1 with the TATA-binding protein (TBP) subunit of TFIID occurs in vivo. In addition, Dr1 can repress transcription from TATA-containing as well as TATA-less promoters in transient transfection assays. Importantly, Dr1-mediated repression can be reversed by overexpression of TBP in vivo. By use of diverse approaches, we mapped two distinct domains in Dr1 required for repression. One domain is essential for the Dr1-TBP interaction, and the second is rich in alanine residues. The TBP-binding domain of Dr1 cannot be replaced by a heterologous DNA-binding domain in mediating repression. We demonstrate that some, but not all, transcriptional activators can reverse Dr1-mediated repression in vivo. |
| doi_str_mv | 10.1101/gad.8.17.2097 |
| format | Article |
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Biochemical analyses reveal that Dr1 directly interacts with the multiprotein TFIID complex. By use of the yeast two-hybrid system, we demonstrate that the association of Dr1 with the TATA-binding protein (TBP) subunit of TFIID occurs in vivo. In addition, Dr1 can repress transcription from TATA-containing as well as TATA-less promoters in transient transfection assays. Importantly, Dr1-mediated repression can be reversed by overexpression of TBP in vivo. By use of diverse approaches, we mapped two distinct domains in Dr1 required for repression. One domain is essential for the Dr1-TBP interaction, and the second is rich in alanine residues. The TBP-binding domain of Dr1 cannot be replaced by a heterologous DNA-binding domain in mediating repression. 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Biochemical analyses reveal that Dr1 directly interacts with the multiprotein TFIID complex. By use of the yeast two-hybrid system, we demonstrate that the association of Dr1 with the TATA-binding protein (TBP) subunit of TFIID occurs in vivo. In addition, Dr1 can repress transcription from TATA-containing as well as TATA-less promoters in transient transfection assays. Importantly, Dr1-mediated repression can be reversed by overexpression of TBP in vivo. By use of diverse approaches, we mapped two distinct domains in Dr1 required for repression. One domain is essential for the Dr1-TBP interaction, and the second is rich in alanine residues. The TBP-binding domain of Dr1 cannot be replaced by a heterologous DNA-binding domain in mediating repression. We demonstrate that some, but not all, transcriptional activators can reverse Dr1-mediated repression in vivo.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>DNA Primers - genetics</subject><subject>Gene Expression Regulation</subject><subject>Genes, MHC Class II</subject><subject>Genetic Vectors</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>TATA Box</subject><subject>Trans-Activators - genetics</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LxDAQQIMouq4ePQo5eeuaSdt8HP12QVBwPYc0na6RNl2TVhD88XZx8TQwPN4Mj5AzYAsABpdrWy_UAuSCMy33yAzKQmdlIeU-mTGlWaZzoY_IcUofjDHBhDgkh1KXSimYkZ_XIY5uGCNmzRjc4PtAbbDtd_KJ9g0d3pGurl-yyofahzXdxH5AH-htBBrxC22bqKUduncbfOpo08dpv4mY0lY1GVxrU6LLJV1jQDpEG5KLfrO9dEIOmkmAp7s5J2_3d6ubx-zp-WF5c_WUOV5wmUHNeSXQWYk2L3NQeS3KChxUlRZYIgBiUWgntHC80kXdFJyh0Cp3lkFt8zm5-PNO33-OmAbT-eSwbW3AfkxGCsX5FGQCsz_QxT6liI3ZRN_Z-G2AmW1tM9U2yoA029oTf74Tj1WH9T-9y5v_AqepfOw</recordid><startdate>19940901</startdate><enddate>19940901</enddate><creator>Yeung, K C</creator><creator>Inostroza, J A</creator><creator>Mermelstein, F H</creator><creator>Kannabiran, C</creator><creator>Reinberg, D</creator><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>7X8</scope></search><sort><creationdate>19940901</creationdate><title>Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription</title><author>Yeung, K C ; Inostroza, J A ; Mermelstein, F H ; Kannabiran, C ; Reinberg, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2427-1d22b6eca7ea353183d65b1c1bb96e5e11ee449c696c2b94df420e6983ca01da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>DNA Primers - genetics</topic><topic>Gene Expression Regulation</topic><topic>Genes, MHC Class II</topic><topic>Genetic Vectors</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>TATA Box</topic><topic>Trans-Activators - genetics</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yeung, K C</creatorcontrib><creatorcontrib>Inostroza, J A</creatorcontrib><creatorcontrib>Mermelstein, F H</creatorcontrib><creatorcontrib>Kannabiran, C</creatorcontrib><creatorcontrib>Reinberg, D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Genes & development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yeung, K C</au><au>Inostroza, J A</au><au>Mermelstein, F H</au><au>Kannabiran, C</au><au>Reinberg, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription</atitle><jtitle>Genes & development</jtitle><addtitle>Genes Dev</addtitle><date>1994-09-01</date><risdate>1994</risdate><volume>8</volume><issue>17</issue><spage>2097</spage><epage>2109</epage><pages>2097-2109</pages><issn>0890-9369</issn><eissn>1549-5477</eissn><abstract>Dr1, a repressor of class II genes, regulates transcription by a novel mechanism. Biochemical analyses reveal that Dr1 directly interacts with the multiprotein TFIID complex. By use of the yeast two-hybrid system, we demonstrate that the association of Dr1 with the TATA-binding protein (TBP) subunit of TFIID occurs in vivo. In addition, Dr1 can repress transcription from TATA-containing as well as TATA-less promoters in transient transfection assays. Importantly, Dr1-mediated repression can be reversed by overexpression of TBP in vivo. By use of diverse approaches, we mapped two distinct domains in Dr1 required for repression. One domain is essential for the Dr1-TBP interaction, and the second is rich in alanine residues. The TBP-binding domain of Dr1 cannot be replaced by a heterologous DNA-binding domain in mediating repression. We demonstrate that some, but not all, transcriptional activators can reverse Dr1-mediated repression in vivo.</abstract><cop>United States</cop><pmid>7958881</pmid><doi>10.1101/gad.8.17.2097</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Genes & development, 1994-09, Vol.8 (17), p.2097-2109 |
| issn | 0890-9369 1549-5477 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence Base Sequence DNA Primers - genetics Gene Expression Regulation Genes, MHC Class II Genetic Vectors HeLa Cells Humans Molecular Sequence Data Phosphoproteins - genetics Phosphoproteins - metabolism Repressor Proteins - genetics Repressor Proteins - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism TATA Box Trans-Activators - genetics Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic |
| title | Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription |
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