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| | ==Structure of the Mediator Head Module from S. cerevisiae== | | ==Structure of the Mediator Head Module from S. cerevisiae== |
| - | <StructureSection load='4gwp' size='340' side='right' caption='[[4gwp]], [[Resolution|resolution]] 4.20Å' scene=''> | + | <StructureSection load='4gwp' size='340' side='right'caption='[[4gwp]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gwp]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GWP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gwp]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GWP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rj1|3rj1]], [[2hzm|2hzm]], [[2hzs|2hzs]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwp OCA], [http://pdbe.org/4gwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gwp RCSB], [http://www.ebi.ac.uk/pdbsum/4gwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gwp ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwp OCA], [https://pdbe.org/4gwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gwp RCSB], [https://www.ebi.ac.uk/pdbsum/4gwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gwp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MED20_YEAST MED20_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:16076843</ref> <ref>PMID:16109375</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> [[http://www.uniprot.org/uniprot/MED22_YEAST MED22_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> [[http://www.uniprot.org/uniprot/MED11_YEAST MED11_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:18691966</ref> [[http://www.uniprot.org/uniprot/MED8_YEAST MED8_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. MED8 binds to the consensus sequence 5'-[AC][AG]GAAAT-3' in both the UAS of SUC2 and the DRS2 of HXK2.<ref>PMID:9918841</ref> <ref>PMID:10526178</ref> <ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> [[http://www.uniprot.org/uniprot/MED6_YEAST MED6_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9234719</ref> <ref>PMID:9845373</ref> [[http://www.uniprot.org/uniprot/MED17_YEAST MED17_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9845373</ref> [[http://www.uniprot.org/uniprot/MED18_YEAST MED18_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:9845373</ref> <ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16109375</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> | + | [https://www.uniprot.org/uniprot/MED11_YEAST MED11_YEAST] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:18691966</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
| + | |
| - | The X-ray crystal structure of the Head module, one-third of the Mediator of transcriptional regulation, has been determined as a complex with the C-terminal domain (CTD) of RNA polymerase II. The structure reveals multiple points of interaction with an extended conformation of the CTD; it suggests a basis for regulation by phosphorylation of the CTD. Biochemical studies show a requirement for Mediator-CTD interaction for transcription.
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| - | | + | |
| - | Structure of the Mediator Head module bound to the carboxy-terminal domain of RNA polymerase II.,Robinson PJ, Bushnell DA, Trnka MJ, Burlingame AL, Kornberg RD Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17931-5. doi:, 10.1073/pnas.1215241109. Epub 2012 Oct 15. PMID:23071300<ref>PMID:23071300</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4gwp" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Saccharomyces cerevisiae]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Burlingame, A L]] | + | [[Category: Burlingame AL]] |
| - | [[Category: Bushnell, D A]] | + | [[Category: Bushnell DA]] |
| - | [[Category: Kornberg, R D]] | + | [[Category: Kornberg RD]] |
| - | [[Category: Robinson, P J.J]] | + | [[Category: Robinson PJJ]] |
| - | [[Category: Trnka, M J]] | + | [[Category: Trnka MJ]] |
| - | [[Category: Binding site]]
| + | |
| - | [[Category: Mediator complex]]
| + | |
| - | [[Category: Model]]
| + | |
| - | [[Category: Molecular]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein structure]]
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| - | [[Category: Protein subunit]]
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| - | [[Category: Rna polymerase ii]]
| + | |
| - | [[Category: Structure-activity relationship]]
| + | |
| - | [[Category: Tertiary]]
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| - | [[Category: Transcription]]
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