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Architecture of the RNA polymerase II-Mediator core initiation complex
The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed...
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| Published in: | Nature (London) 2015-02, Vol.518 (7539), p.376-380 |
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| container_end_page | 380 |
| container_issue | 7539 |
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| creator | Plaschka, C Larivière, L Wenzeck, L Seizl, M Hemann, M Tegunov, D Petrotchenko, E V Borchers, C H Baumeister, W Herzog, F Villa, E Cramer, P |
| description | The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed bound to a core initiation complex was determined at 9.7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD). The Mediator head module binds the Pol II dock and the TFIIB ribbon and stabilizes the initiation complex. The Mediator middle module extends to the Pol II foot with a 'plank' that may influence polymerase conformation. The Mediator subunit Med14 forms a 'beam' between the head and middle modules and connects to the tail module that is predicted to bind transcription activators located on upstream DNA. The Mediator 'arm' and 'hook' domains contribute to a 'cradle' that may position the CTD and TFIIH kinase to stimulate Pol II phosphorylation. |
| doi_str_mv | 10.1038/nature14229 |
| format | article |
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Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed bound to a core initiation complex was determined at 9.7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD). The Mediator head module binds the Pol II dock and the TFIIB ribbon and stabilizes the initiation complex. The Mediator middle module extends to the Pol II foot with a 'plank' that may influence polymerase conformation. The Mediator subunit Med14 forms a 'beam' between the head and middle modules and connects to the tail module that is predicted to bind transcription activators located on upstream DNA. The Mediator 'arm' and 'hook' domains contribute to a 'cradle' that may position the CTD and TFIIH kinase to stimulate Pol II phosphorylation.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature14229</identifier><identifier>PMID: 25652824</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>England: Nature Publishing Group</publisher><subject>Allosteric Regulation ; Binding Sites ; Cryoelectron Microscopy ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - metabolism ; Enzyme Activation ; Genetic transcription ; Kinases ; Mediator Complex - chemistry ; Mediator Complex - metabolism ; Mediator Complex - ultrastructure ; Microscopy ; Models, Molecular ; Phosphorylation ; Physiological aspects ; Protein research ; Protein Stability ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; RNA polymerase ; RNA Polymerase II - chemistry ; RNA Polymerase II - metabolism ; RNA Polymerase II - ultrastructure ; RNA polymerases ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - ultrastructure ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Saccharomyces cerevisiae Proteins - ultrastructure ; Transcription Factor TFIIB - chemistry ; Transcription Factor TFIIB - metabolism ; Transcription Factor TFIIH - chemistry ; Transcription Factor TFIIH - metabolism ; Transcription factors ; Transcription Initiation, Genetic ; Yeast</subject><ispartof>Nature (London), 2015-02, Vol.518 (7539), p.376-380</ispartof><rights>COPYRIGHT 2015 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 19, 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c586t-1c08fdd1a48a374ebac9e5aa483956fb674262cbaca4c6784a922d43894a6fdf3</citedby><cites>FETCH-LOGICAL-c586t-1c08fdd1a48a374ebac9e5aa483956fb674262cbaca4c6784a922d43894a6fdf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25652824$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Plaschka, C</creatorcontrib><creatorcontrib>Larivière, L</creatorcontrib><creatorcontrib>Wenzeck, L</creatorcontrib><creatorcontrib>Seizl, M</creatorcontrib><creatorcontrib>Hemann, M</creatorcontrib><creatorcontrib>Tegunov, D</creatorcontrib><creatorcontrib>Petrotchenko, E V</creatorcontrib><creatorcontrib>Borchers, C H</creatorcontrib><creatorcontrib>Baumeister, W</creatorcontrib><creatorcontrib>Herzog, F</creatorcontrib><creatorcontrib>Villa, E</creatorcontrib><creatorcontrib>Cramer, P</creatorcontrib><title>Architecture of the RNA polymerase II-Mediator core initiation complex</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed bound to a core initiation complex was determined at 9.7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD). The Mediator head module binds the Pol II dock and the TFIIB ribbon and stabilizes the initiation complex. The Mediator middle module extends to the Pol II foot with a 'plank' that may influence polymerase conformation. The Mediator subunit Med14 forms a 'beam' between the head and middle modules and connects to the tail module that is predicted to bind transcription activators located on upstream DNA. The Mediator 'arm' and 'hook' domains contribute to a 'cradle' that may position the CTD and TFIIH kinase to stimulate Pol II phosphorylation.</description><subject>Allosteric Regulation</subject><subject>Binding Sites</subject><subject>Cryoelectron Microscopy</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>Enzyme Activation</subject><subject>Genetic transcription</subject><subject>Kinases</subject><subject>Mediator Complex - chemistry</subject><subject>Mediator Complex - metabolism</subject><subject>Mediator Complex - ultrastructure</subject><subject>Microscopy</subject><subject>Models, Molecular</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein research</subject><subject>Protein Stability</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>RNA polymerase</subject><subject>RNA Polymerase II - 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Plaschka, C</au><au>Larivière, L</au><au>Wenzeck, L</au><au>Seizl, M</au><au>Hemann, M</au><au>Tegunov, D</au><au>Petrotchenko, E V</au><au>Borchers, C H</au><au>Baumeister, W</au><au>Herzog, F</au><au>Villa, E</au><au>Cramer, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Architecture of the RNA polymerase II-Mediator core initiation complex</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>2015-02-19</date><risdate>2015</risdate><volume>518</volume><issue>7539</issue><spage>376</spage><epage>380</epage><pages>376-380</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed bound to a core initiation complex was determined at 9.7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD). The Mediator head module binds the Pol II dock and the TFIIB ribbon and stabilizes the initiation complex. The Mediator middle module extends to the Pol II foot with a 'plank' that may influence polymerase conformation. The Mediator subunit Med14 forms a 'beam' between the head and middle modules and connects to the tail module that is predicted to bind transcription activators located on upstream DNA. The Mediator 'arm' and 'hook' domains contribute to a 'cradle' that may position the CTD and TFIIH kinase to stimulate Pol II phosphorylation.</abstract><cop>England</cop><pub>Nature Publishing Group</pub><pmid>25652824</pmid><doi>10.1038/nature14229</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2015-02, Vol.518 (7539), p.376-380 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | Nature_系列刊 |
| subjects | Allosteric Regulation Binding Sites Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism Enzyme Activation Genetic transcription Kinases Mediator Complex - chemistry Mediator Complex - metabolism Mediator Complex - ultrastructure Microscopy Models, Molecular Phosphorylation Physiological aspects Protein research Protein Stability Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - metabolism RNA polymerase RNA Polymerase II - chemistry RNA Polymerase II - metabolism RNA Polymerase II - ultrastructure RNA polymerases Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Transcription Factor TFIIB - chemistry Transcription Factor TFIIB - metabolism Transcription Factor TFIIH - chemistry Transcription Factor TFIIH - metabolism Transcription factors Transcription Initiation, Genetic Yeast |
| title | Architecture of the RNA polymerase II-Mediator core initiation complex |
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