Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation
General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-03, Vol.109 (13), p.4816-4821 |
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creator | Murakami, Kenji Gibbons, Brian J Davis, Ralph E Nagai, Shigeki Liu, Xin Robinson, Philip J. J Wu, Tinghe Kaplan, Craig D Kornberg, Roger D |
description | General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with the Ssl2 subunit, a DNA helicase that drives promoter melting for the initiation of transcription. Tfb6 does not, however, dissociate Ssl2 from TFIIH in the context of a fully assembled transcription preinitiation complex. Our findings suggest a dynamic state of Ssl2, allowing its engagement in multiple cellular processes. |
doi_str_mv | 10.1073/pnas.1201448109 |
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J ; Wu, Tinghe ; Kaplan, Craig D ; Kornberg, Roger D</creator><creatorcontrib>Murakami, Kenji ; Gibbons, Brian J ; Davis, Ralph E ; Nagai, Shigeki ; Liu, Xin ; Robinson, Philip J. J ; Wu, Tinghe ; Kaplan, Craig D ; Kornberg, Roger D</creatorcontrib><description>General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with the Ssl2 subunit, a DNA helicase that drives promoter melting for the initiation of transcription. Tfb6 does not, however, dissociate Ssl2 from TFIIH in the context of a fully assembled transcription preinitiation complex. Our findings suggest a dynamic state of Ssl2, allowing its engagement in multiple cellular processes.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1201448109</identifier><identifier>PMID: 22411836</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Acetates ; Alleles ; Biological Sciences ; Cells ; Chemical compounds ; Chromatography ; Chromatography, Liquid ; dissociation ; DNA ; DNA helicases ; DNA Helicases - metabolism ; DNA repair ; Gene Deletion ; Gene Expression Regulation, Fungal - radiation effects ; General transcription factors ; Humans ; Mass Spectrometry ; melting ; Messenger RNA ; Molecules ; Pharmacology ; Phenotype ; Phosphorylation - radiation effects ; Potassium ; Protein Binding - radiation effects ; Protein Subunits - metabolism ; RNA ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - radiation effects ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Signal transduction ; Temperature ; Transcription Factor TFIIH - chemistry ; Transcription Factor TFIIH - metabolism ; transcription factors ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Transcription, Genetic - radiation effects ; Ultraviolet Rays ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-03, Vol.109 (13), p.4816-4821</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 27, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-3afca849b0a9560f98113685faeb7053701773e17fae582f8b38fcf6cdce92d93</citedby><cites>FETCH-LOGICAL-c522t-3afca849b0a9560f98113685faeb7053701773e17fae582f8b38fcf6cdce92d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/13.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41588379$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41588379$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22411836$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murakami, Kenji</creatorcontrib><creatorcontrib>Gibbons, Brian J</creatorcontrib><creatorcontrib>Davis, Ralph E</creatorcontrib><creatorcontrib>Nagai, Shigeki</creatorcontrib><creatorcontrib>Liu, Xin</creatorcontrib><creatorcontrib>Robinson, Philip J. J</creatorcontrib><creatorcontrib>Wu, Tinghe</creatorcontrib><creatorcontrib>Kaplan, Craig D</creatorcontrib><creatorcontrib>Kornberg, Roger D</creatorcontrib><title>Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with the Ssl2 subunit, a DNA helicase that drives promoter melting for the initiation of transcription. Tfb6 does not, however, dissociate Ssl2 from TFIIH in the context of a fully assembled transcription preinitiation complex. Our findings suggest a dynamic state of Ssl2, allowing its engagement in multiple cellular processes.</description><subject>Acetates</subject><subject>Alleles</subject><subject>Biological Sciences</subject><subject>Cells</subject><subject>Chemical compounds</subject><subject>Chromatography</subject><subject>Chromatography, Liquid</subject><subject>dissociation</subject><subject>DNA</subject><subject>DNA helicases</subject><subject>DNA Helicases - metabolism</subject><subject>DNA repair</subject><subject>Gene Deletion</subject><subject>Gene Expression Regulation, Fungal - radiation effects</subject><subject>General transcription factors</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>melting</subject><subject>Messenger RNA</subject><subject>Molecules</subject><subject>Pharmacology</subject><subject>Phenotype</subject><subject>Phosphorylation - radiation effects</subject><subject>Potassium</subject><subject>Protein Binding - radiation effects</subject><subject>Protein Subunits - metabolism</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - radiation effects</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal transduction</subject><subject>Temperature</subject><subject>Transcription Factor TFIIH - chemistry</subject><subject>Transcription Factor TFIIH - metabolism</subject><subject>transcription factors</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic - radiation effects</subject><subject>Ultraviolet Rays</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkk9vFCEYxonR2LV69qSSnjx0Wv7NDFyamMbaTZp46PZMGAZ22czCCkyTfha_bBl33dVeXvLCj4cHHgD4iNEFRi293HqVLjBBmDGOkXgFZqXiqmECvQYzhEhbcUbYCXiX0hohJGqO3oITQhjGnDYz8Hthu-YcKriN5tGFMQ1PcPSuNz4760wP09iVPsNgYV4ZuDTeRDXAHJVPOrptdsFDq3QOES5u5vPb86lzg8sqmwR7l1LQTv3BisZ9GghcmcFplQxUNpv4QsuV03b8e_DGqiGZD_vxFDzcfF9c31Z3P3_Mr7_dVbomJFdUWa04Ex1Som6QFRxj2vDaKtO1qKYtwm1LDW7LRM2J5R3lVttG99oI0gt6Cq52utux25gy64ujQW6j26j4JINy8v8V71ZyGR4lpYQKPgl83QvE8Gs0KcuNS9oMg_KmPKnEiCDOcDFX0LMX6DqM0ZfrSVGzhvMWswJd7iAdQ0rR2IMXjOSUu5xyl8fcy47P_17hwP8NugBf9sC08ygnJKayaEzEpx2xTiXLA1Jsc05bcVSwKki1jC7Jh_vJQflWvNSGPgNd58pJ</recordid><startdate>20120327</startdate><enddate>20120327</enddate><creator>Murakami, Kenji</creator><creator>Gibbons, Brian J</creator><creator>Davis, Ralph E</creator><creator>Nagai, Shigeki</creator><creator>Liu, Xin</creator><creator>Robinson, Philip J. 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J</au><au>Wu, Tinghe</au><au>Kaplan, Craig D</au><au>Kornberg, Roger D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-03-27</date><risdate>2012</risdate><volume>109</volume><issue>13</issue><spage>4816</spage><epage>4821</epage><pages>4816-4821</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with the Ssl2 subunit, a DNA helicase that drives promoter melting for the initiation of transcription. Tfb6 does not, however, dissociate Ssl2 from TFIIH in the context of a fully assembled transcription preinitiation complex. Our findings suggest a dynamic state of Ssl2, allowing its engagement in multiple cellular processes.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22411836</pmid><doi>10.1073/pnas.1201448109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Acetates Alleles Biological Sciences Cells Chemical compounds Chromatography Chromatography, Liquid dissociation DNA DNA helicases DNA Helicases - metabolism DNA repair Gene Deletion Gene Expression Regulation, Fungal - radiation effects General transcription factors Humans Mass Spectrometry melting Messenger RNA Molecules Pharmacology Phenotype Phosphorylation - radiation effects Potassium Protein Binding - radiation effects Protein Subunits - metabolism RNA RNA, Messenger - genetics RNA, Messenger - metabolism Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - radiation effects Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Signal transduction Temperature Transcription Factor TFIIH - chemistry Transcription Factor TFIIH - metabolism transcription factors Transcription Factors - chemistry Transcription Factors - metabolism Transcription, Genetic - radiation effects Ultraviolet Rays Yeasts |
title | Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation |
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