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| | <StructureSection load='3vp8' size='340' side='right'caption='[[3vp8]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='3vp8' size='340' side='right'caption='[[3vp8]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vp8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VP8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vp8]] is a 4 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=3VP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VP8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vp9|3vp9]]</div></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]] 1.91Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TUP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp8 OCA], [https://pdbe.org/3vp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vp8 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=3vp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp8 OCA], [https://pdbe.org/3vp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vp8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TUP1_YEAST TUP1_YEAST]] Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.<ref>PMID:2247069</ref> <ref>PMID:11069890</ref> <ref>PMID:10722672</ref> <ref>PMID:11230135</ref> <ref>PMID:11172717</ref> <ref>PMID:11784848</ref> <ref>PMID:14665463</ref>
| + | [https://www.uniprot.org/uniprot/TUP1_YEAST TUP1_YEAST] Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.<ref>PMID:2247069</ref> <ref>PMID:11069890</ref> <ref>PMID:10722672</ref> <ref>PMID:11230135</ref> <ref>PMID:11172717</ref> <ref>PMID:11784848</ref> <ref>PMID:14665463</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The yeast Cyc8p-Tup1p protein complex is a general transcriptional corepressor of genes involved in many different physiological processes. Herein, we present the crystal structure of the Tup1p N-terminal domain (residues 1-92), essential for Tup1p self-assembly and interaction with Cyc8p. This domain tetramerizes to form a novel antiparallel four-helix bundle. Coiled coil interactions near the helical ends hold each dimer together, whereas interdimeric association involves only two sets of two residues located toward the chain centers. A mutagenesis study confirmed that the nonpolar residues responsible for the association of the protomers as dimers are also required for transcriptional repression. An additional structural study demonstrated that the domain containing an Leu(62) --> Arg mutation that had been shown not to bind Cyc8p exhibits an altered structure, distinct from the wild type. This altered structure explains why the mutant cannot bind Cyc8p. The data presented herein highlight the importance of the architecture of the Tup1p N-terminal domain for self-association.
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| - | | + | |
| - | Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p and its functional implications.,Matsumura H, Kusaka N, Nakamura T, Tanaka N, Sagegami K, Uegaki K, Inoue T, Mukai Y J Biol Chem. 2012 Aug 3;287(32):26528-38. Epub 2012 Jun 15. PMID:22707714<ref>PMID:22707714</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3vp8" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Inoue, T]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Kusaka, N]] | + | [[Category: Inoue T]] |
| - | [[Category: Matsumura, H]] | + | [[Category: Kusaka N]] |
| - | [[Category: Mukai, Y]] | + | [[Category: Matsumura H]] |
| - | [[Category: Nakamura, T]] | + | [[Category: Mukai Y]] |
| - | [[Category: Sagegami, K]] | + | [[Category: Nakamura T]] |
| - | [[Category: Tanaka, N]] | + | [[Category: Sagegami K]] |
| - | [[Category: Uegaki, K]] | + | [[Category: Tanaka N]] |
| - | [[Category: Four helix bundle]]
| + | [[Category: Uegaki K]] |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
TUP1_YEAST Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.[1] [2] [3] [4] [5] [6] [7]
References
- ↑ Williams FE, Trumbly RJ. Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae. Mol Cell Biol. 1990 Dec;10(12):6500-11. PMID:2247069
- ↑ Watson AD, Edmondson DG, Bone JR, Mukai Y, Yu Y, Du W, Stillman DJ, Roth SY. Ssn6-Tup1 interacts with class I histone deacetylases required for repression. Genes Dev. 2000 Nov 1;14(21):2737-44. PMID:11069890
- ↑ Papamichos-Chronakis M, Conlan RS, Gounalaki N, Copf T, Tzamarias D. Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme. J Biol Chem. 2000 Mar 24;275(12):8397-403. PMID:10722672
- ↑ Proft M, Pascual-Ahuir A, de Nadal E, Arino J, Serrano R, Posas F. Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress. EMBO J. 2001 Mar 1;20(5):1123-33. PMID:11230135 doi:10.1093/emboj/20.5.1123
- ↑ Wu J, Suka N, Carlson M, Grunstein M. TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Mol Cell. 2001 Jan;7(1):117-26. PMID:11172717
- ↑ Davie JK, Trumbly RJ, Dent SY. Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo. Mol Cell Biol. 2002 Feb;22(3):693-703. PMID:11784848
- ↑ Mennella TA, Klinkenberg LG, Zitomer RS. Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein. Eukaryot Cell. 2003 Dec;2(6):1288-303. PMID:14665463
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