Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription
Recent evidence suggests that transcription initiation by all three eukaryotic RNA polymerases involves a complex of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here, we map the functional domains of the nucleolar HMG box protein hUBF, which binds to the human rRNA pro...
Gespeichert in:
Veröffentlicht in: | Genes & development 1992-10, Vol.6 (10), p.1950-1963 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1963 |
---|---|
container_issue | 10 |
container_start_page | 1950 |
container_title | Genes & development |
container_volume | 6 |
creator | JANTZEN, H.-M MING CHOW, A KING, D. S TJIAN, R |
description | Recent evidence suggests that transcription initiation by all three eukaryotic RNA polymerases involves a complex of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here, we map the functional domains of the nucleolar HMG box protein hUBF, which binds to the human rRNA promoter and stimulates transcription by RNA polymerase I through cooperative interactions with a distinct TBP-TAF complex, hSL1. DNase I footprint analysis of mutant hUBF proteins and of a synthetic peptide of 84 amino acids reveals that HMG box 1 is necessary and sufficient for DNA sequence specificity, whereas other HMG boxes and the amino terminus modulate the binding efficiency. hUBF contains multiple activation domains that include the acidic carboxyl terminus and three HMG boxes. HMG boxes 3 and 4 and the acidic tail contribute significantly to an extended footprinting pattern in the presence of hSL1, suggestive of specific protein-protein interactions. Moreover, the inability of xUBF from Xenopus laevis to form an initiation complex with hSL1 can be overcome by hybrid proteins containing human HMG box 4 and the acidic carboxyl terminus. These results strongly suggest an important role of transcription activation domains of hUBF in mediating interactions with the TBP-TAF complex hSL1. |
doi_str_mv | 10.1101/gad.6.10.1950 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73226123</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16411552</sourcerecordid><originalsourceid>FETCH-LOGICAL-c387t-d983428b61b49137c21f82fbcf2afc78cfcc7cb9c37ff1884cee8239bdcba42f3</originalsourceid><addsrcrecordid>eNqFkc1v1DAQxS1UVJbCkSOSD6i3LP5I_HFcVi1UWkCC7TlyJnbXKIlT21vonT8ct7sqx55Go_ebp5l5CL2jZEkpoR9vTL8Uy4dON-QFWtCm1lVTS3mCFkRpUmku9Cv0OqVfhBBBhDhFp5RrRSRboL9f90P282BxH0bjp4SDw3ln8Y9vKzyH4X600SSLr7CB7O9MDhHvrj9dYj_lokDGv33ePU5sV9tV1fmp99MNnmPI1k8YwljM_-Ddzw3FOeDR9t5ki3M0U4Lo5-zD9Aa9dGZI9u2xnqHry4vt-ku1-f75ar3aVMCVzFWvFa-Z6gTtak25BEadYq4Dx4wDqcABSOg0cOkcVaoGaxXjuuuhMzVz_AydH3zLdrd7m3I7-gR2GMxkwz61kjMmKOPPglTUlDYNK2B1ACGGlKJ17Rz9aOJ9S0n7EE9b4mnFY1fiKfz7o_G-K6_4Tx_yKPqHo24SmMGVL4FPT1jNBSkX8X_QV5mu</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16411552</pqid></control><display><type>article</type><title>Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>JANTZEN, H.-M ; MING CHOW, A ; KING, D. S ; TJIAN, R</creator><creatorcontrib>JANTZEN, H.-M ; MING CHOW, A ; KING, D. S ; TJIAN, R</creatorcontrib><description>Recent evidence suggests that transcription initiation by all three eukaryotic RNA polymerases involves a complex of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here, we map the functional domains of the nucleolar HMG box protein hUBF, which binds to the human rRNA promoter and stimulates transcription by RNA polymerase I through cooperative interactions with a distinct TBP-TAF complex, hSL1. DNase I footprint analysis of mutant hUBF proteins and of a synthetic peptide of 84 amino acids reveals that HMG box 1 is necessary and sufficient for DNA sequence specificity, whereas other HMG boxes and the amino terminus modulate the binding efficiency. hUBF contains multiple activation domains that include the acidic carboxyl terminus and three HMG boxes. HMG boxes 3 and 4 and the acidic tail contribute significantly to an extended footprinting pattern in the presence of hSL1, suggestive of specific protein-protein interactions. Moreover, the inability of xUBF from Xenopus laevis to form an initiation complex with hSL1 can be overcome by hybrid proteins containing human HMG box 4 and the acidic carboxyl terminus. These results strongly suggest an important role of transcription activation domains of hUBF in mediating interactions with the TBP-TAF complex hSL1.</description><identifier>ISSN: 0890-9369</identifier><identifier>EISSN: 1549-5477</identifier><identifier>DOI: 10.1101/gad.6.10.1950</identifier><identifier>PMID: 1398072</identifier><identifier>CODEN: GEDEEP</identifier><language>eng</language><publisher>Cold Spring Harbor, NY: Cold Spring Harbor Laboratory</publisher><subject>Animals ; Base Sequence ; Biological and medical sciences ; DNA - metabolism ; DNA-Binding Proteins - metabolism ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; Humans ; Hybrid Cells ; Macromolecular Substances ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Plasmids ; Pol1 Transcription Initiation Complex Proteins ; Promoter Regions, Genetic ; Protein Binding ; Protein Biosynthesis ; RNA Polymerase I - metabolism ; RNA, Ribosomal - genetics ; TATA Box ; TATA-Box Binding Protein ; Transcription Factors - metabolism ; Transcription, Genetic ; Transcription. Transcription factor. Splicing. Rna processing ; Xenopus laevis</subject><ispartof>Genes & development, 1992-10, Vol.6 (10), p.1950-1963</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c387t-d983428b61b49137c21f82fbcf2afc78cfcc7cb9c37ff1884cee8239bdcba42f3</citedby><cites>FETCH-LOGICAL-c387t-d983428b61b49137c21f82fbcf2afc78cfcc7cb9c37ff1884cee8239bdcba42f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4360823$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1398072$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>JANTZEN, H.-M</creatorcontrib><creatorcontrib>MING CHOW, A</creatorcontrib><creatorcontrib>KING, D. S</creatorcontrib><creatorcontrib>TJIAN, R</creatorcontrib><title>Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription</title><title>Genes & development</title><addtitle>Genes Dev</addtitle><description>Recent evidence suggests that transcription initiation by all three eukaryotic RNA polymerases involves a complex of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here, we map the functional domains of the nucleolar HMG box protein hUBF, which binds to the human rRNA promoter and stimulates transcription by RNA polymerase I through cooperative interactions with a distinct TBP-TAF complex, hSL1. DNase I footprint analysis of mutant hUBF proteins and of a synthetic peptide of 84 amino acids reveals that HMG box 1 is necessary and sufficient for DNA sequence specificity, whereas other HMG boxes and the amino terminus modulate the binding efficiency. hUBF contains multiple activation domains that include the acidic carboxyl terminus and three HMG boxes. HMG boxes 3 and 4 and the acidic tail contribute significantly to an extended footprinting pattern in the presence of hSL1, suggestive of specific protein-protein interactions. Moreover, the inability of xUBF from Xenopus laevis to form an initiation complex with hSL1 can be overcome by hybrid proteins containing human HMG box 4 and the acidic carboxyl terminus. These results strongly suggest an important role of transcription activation domains of hUBF in mediating interactions with the TBP-TAF complex hSL1.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hybrid Cells</subject><subject>Macromolecular Substances</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Plasmids</subject><subject>Pol1 Transcription Initiation Complex Proteins</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Protein Biosynthesis</subject><subject>RNA Polymerase I - metabolism</subject><subject>RNA, Ribosomal - genetics</subject><subject>TATA Box</subject><subject>TATA-Box Binding Protein</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Transcription. Transcription factor. Splicing. Rna processing</subject><subject>Xenopus laevis</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS1UVJbCkSOSD6i3LP5I_HFcVi1UWkCC7TlyJnbXKIlT21vonT8ct7sqx55Go_ebp5l5CL2jZEkpoR9vTL8Uy4dON-QFWtCm1lVTS3mCFkRpUmku9Cv0OqVfhBBBhDhFp5RrRSRboL9f90P282BxH0bjp4SDw3ln8Y9vKzyH4X600SSLr7CB7O9MDhHvrj9dYj_lokDGv33ePU5sV9tV1fmp99MNnmPI1k8YwljM_-Ddzw3FOeDR9t5ki3M0U4Lo5-zD9Aa9dGZI9u2xnqHry4vt-ku1-f75ar3aVMCVzFWvFa-Z6gTtak25BEadYq4Dx4wDqcABSOg0cOkcVaoGaxXjuuuhMzVz_AydH3zLdrd7m3I7-gR2GMxkwz61kjMmKOPPglTUlDYNK2B1ACGGlKJ17Rz9aOJ9S0n7EE9b4mnFY1fiKfz7o_G-K6_4Tx_yKPqHo24SmMGVL4FPT1jNBSkX8X_QV5mu</recordid><startdate>19921001</startdate><enddate>19921001</enddate><creator>JANTZEN, H.-M</creator><creator>MING CHOW, A</creator><creator>KING, D. S</creator><creator>TJIAN, R</creator><general>Cold Spring Harbor Laboratory</general><scope>IQODW</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19921001</creationdate><title>Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription</title><author>JANTZEN, H.-M ; MING CHOW, A ; KING, D. S ; TJIAN, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c387t-d983428b61b49137c21f82fbcf2afc78cfcc7cb9c37ff1884cee8239bdcba42f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hybrid Cells</topic><topic>Macromolecular Substances</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Plasmids</topic><topic>Pol1 Transcription Initiation Complex Proteins</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Binding</topic><topic>Protein Biosynthesis</topic><topic>RNA Polymerase I - metabolism</topic><topic>RNA, Ribosomal - genetics</topic><topic>TATA Box</topic><topic>TATA-Box Binding Protein</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JANTZEN, H.-M</creatorcontrib><creatorcontrib>MING CHOW, A</creatorcontrib><creatorcontrib>KING, D. S</creatorcontrib><creatorcontrib>TJIAN, R</creatorcontrib><collection>Pascal-Francis</collection><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>Genes & development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>JANTZEN, H.-M</au><au>MING CHOW, A</au><au>KING, D. S</au><au>TJIAN, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription</atitle><jtitle>Genes & development</jtitle><addtitle>Genes Dev</addtitle><date>1992-10-01</date><risdate>1992</risdate><volume>6</volume><issue>10</issue><spage>1950</spage><epage>1963</epage><pages>1950-1963</pages><issn>0890-9369</issn><eissn>1549-5477</eissn><coden>GEDEEP</coden><abstract>Recent evidence suggests that transcription initiation by all three eukaryotic RNA polymerases involves a complex of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here, we map the functional domains of the nucleolar HMG box protein hUBF, which binds to the human rRNA promoter and stimulates transcription by RNA polymerase I through cooperative interactions with a distinct TBP-TAF complex, hSL1. DNase I footprint analysis of mutant hUBF proteins and of a synthetic peptide of 84 amino acids reveals that HMG box 1 is necessary and sufficient for DNA sequence specificity, whereas other HMG boxes and the amino terminus modulate the binding efficiency. hUBF contains multiple activation domains that include the acidic carboxyl terminus and three HMG boxes. HMG boxes 3 and 4 and the acidic tail contribute significantly to an extended footprinting pattern in the presence of hSL1, suggestive of specific protein-protein interactions. Moreover, the inability of xUBF from Xenopus laevis to form an initiation complex with hSL1 can be overcome by hybrid proteins containing human HMG box 4 and the acidic carboxyl terminus. These results strongly suggest an important role of transcription activation domains of hUBF in mediating interactions with the TBP-TAF complex hSL1.</abstract><cop>Cold Spring Harbor, NY</cop><pub>Cold Spring Harbor Laboratory</pub><pmid>1398072</pmid><doi>10.1101/gad.6.10.1950</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0890-9369 |
ispartof | Genes & development, 1992-10, Vol.6 (10), p.1950-1963 |
issn | 0890-9369 1549-5477 |
language | eng |
recordid | cdi_proquest_miscellaneous_73226123 |
source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
subjects | Animals Base Sequence Biological and medical sciences DNA - metabolism DNA-Binding Proteins - metabolism Enzyme Activation Fundamental and applied biological sciences. Psychology Humans Hybrid Cells Macromolecular Substances Molecular and cellular biology Molecular genetics Molecular Sequence Data Plasmids Pol1 Transcription Initiation Complex Proteins Promoter Regions, Genetic Protein Binding Protein Biosynthesis RNA Polymerase I - metabolism RNA, Ribosomal - genetics TATA Box TATA-Box Binding Protein Transcription Factors - metabolism Transcription, Genetic Transcription. Transcription factor. Splicing. Rna processing Xenopus laevis |
title | Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T02%3A10%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Multiple%20domains%20of%20the%20RNA%20polymerase%20I%20activator%20hUBF%20interact%20with%20the%20TATA-binding%20protein%20complex%20hSL1%20to%20mediate%20transcription&rft.jtitle=Genes%20&%20development&rft.au=JANTZEN,%20H.-M&rft.date=1992-10-01&rft.volume=6&rft.issue=10&rft.spage=1950&rft.epage=1963&rft.pages=1950-1963&rft.issn=0890-9369&rft.eissn=1549-5477&rft.coden=GEDEEP&rft_id=info:doi/10.1101/gad.6.10.1950&rft_dat=%3Cproquest_cross%3E16411552%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16411552&rft_id=info:pmid/1398072&rfr_iscdi=true |