Structural Organization of Yeast and Mammalian Mediator Complexes
Structures of yeast Mediator complex, of a related complex from mouse cells and of thyroid hormone receptor-associated protein complex from human cells have been determined by three-dimensional reconstruction from electron micrographs of single particles. All three complexes show a division in two p...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-12, Vol.97 (26), p.14307-14310 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Dotson, M R Yuan, C X Roeder, R G Myers, L C Gustafsson, C M Jiang, Y W Li, Y Kornberg, R D Asturias, F J |
| description | Structures of yeast Mediator complex, of a related complex from mouse cells and of thyroid hormone receptor-associated protein complex from human cells have been determined by three-dimensional reconstruction from electron micrographs of single particles. All three complexes show a division in two parts, a "head" domain and a combined "middle-tail" domain. The head domains of the three complexes appear most similar and interact most closely with RNA polymerase II. The middle-tail domains show the greatest structural divergence and, in the case of the tail domain, may not interact with polymerase at all. Consistent with this structural divergence, analysis of a yeast Mediator mutant localizes subunits that are not conserved between yeast and mammalian cells to the tail domain. Biochemically defined Rgr1 and Srb4 modules of yeast Mediator are then assigned to the middle and head domains. |
| doi_str_mv | 10.1073/pnas.260489497 |
| format | Article |
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All three complexes show a division in two parts, a "head" domain and a combined "middle-tail" domain. The head domains of the three complexes appear most similar and interact most closely with RNA polymerase II. The middle-tail domains show the greatest structural divergence and, in the case of the tail domain, may not interact with polymerase at all. Consistent with this structural divergence, analysis of a yeast Mediator mutant localizes subunits that are not conserved between yeast and mammalian cells to the tail domain. Biochemically defined Rgr1 and Srb4 modules of yeast Mediator are then assigned to the middle and head domains.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.260489497</identifier><identifier>PMID: 11114191</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Biochemistry ; Biological Sciences ; Cells ; Cellular biology ; Enzymes ; HeLa Cells ; Humans ; Mammals ; Mediator Complex ; Mice ; Molecules ; Nuclear Proteins - chemistry ; Nuclear Proteins - ultrastructure ; Particle interactions ; Protein Conformation ; Receptors, Thyroid Hormone - metabolism ; Rgr1 protein ; Ribonucleic acid ; RNA ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - chemistry ; Srb4 protein ; thyroid hormone receptors ; Thyroid hormones ; Trans-Activators ; Transcription Factors ; Transcriptional regulatory elements ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-12, Vol.97 (26), p.14307-14310</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 19, 2000</rights><rights>Copyright © 2000, The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-798443da30b6f4b69e19e8007941df5d343dfc7cff4b367182a2adfdabef6c4e3</citedby><cites>FETCH-LOGICAL-c522t-798443da30b6f4b69e19e8007941df5d343dfc7cff4b367182a2adfdabef6c4e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/26.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2666291$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2666291$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11114191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dotson, M R</creatorcontrib><creatorcontrib>Yuan, C X</creatorcontrib><creatorcontrib>Roeder, R G</creatorcontrib><creatorcontrib>Myers, L C</creatorcontrib><creatorcontrib>Gustafsson, C M</creatorcontrib><creatorcontrib>Jiang, Y W</creatorcontrib><creatorcontrib>Li, Y</creatorcontrib><creatorcontrib>Kornberg, R D</creatorcontrib><creatorcontrib>Asturias, F J</creatorcontrib><title>Structural Organization of Yeast and Mammalian Mediator Complexes</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Structures of yeast Mediator complex, of a related complex from mouse cells and of thyroid hormone receptor-associated protein complex from human cells have been determined by three-dimensional reconstruction from electron micrographs of single particles. All three complexes show a division in two parts, a "head" domain and a combined "middle-tail" domain. The head domains of the three complexes appear most similar and interact most closely with RNA polymerase II. The middle-tail domains show the greatest structural divergence and, in the case of the tail domain, may not interact with polymerase at all. Consistent with this structural divergence, analysis of a yeast Mediator mutant localizes subunits that are not conserved between yeast and mammalian cells to the tail domain. 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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Biochemistry Biological Sciences Cells Cellular biology Enzymes HeLa Cells Humans Mammals Mediator Complex Mice Molecules Nuclear Proteins - chemistry Nuclear Proteins - ultrastructure Particle interactions Protein Conformation Receptors, Thyroid Hormone - metabolism Rgr1 protein Ribonucleic acid RNA Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Srb4 protein thyroid hormone receptors Thyroid hormones Trans-Activators Transcription Factors Transcriptional regulatory elements Yeast Yeasts |
| title | Structural Organization of Yeast and Mammalian Mediator Complexes |
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