1erj

From Proteopedia

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Current revision

CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 DOMAIN OF TUP1

Structural highlights

1erj is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Tup1-Ssn6 corepressor complex regulates the expression of several sets of genes, including genes that specify mating type in the yeast Saccharomyces cerevisiae. Repression of mating-type genes occurs when Tup1-Ssn6 is brought to the DNA by the Matalpha2 DNA-binding protein and assembled upstream of a- and haploid-specific genes. We have determined the 2.3 A X-ray crystal structure of the C-terminal domain of Tup1 (accesion No. 1ERJ), a 43 kDa fragment that contains seven copies of the WD40 sequence motif and binds to the Matalpha2 protein. Moreover, this portion of the protein can partially substitute for full-length Tup1 in bringing about transcriptional repression. The structure reveals a seven-bladed beta propeller with an N-terminal subdomain that is anchored to the side of the propeller and extends the beta sheet of one of the blades. Point mutations in Tup1 that specifically affect the Tup1-Matalpha2 interaction cluster on one surface of the propeller. We identified regions of Tup1 that are conserved among the fungal Tup1 homologs and may be important in protein-protein interactions with additional components of the Tup1-mediated repression pathways.

Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast.,Sprague ER, Redd MJ, Johnson AD, Wolberger C EMBO J. 2000 Jun 15;19(12):3016-27. PMID:10856245^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Sprague ER, Redd MJ, Johnson AD, Wolberger C. Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast. EMBO J. 2000 Jun 15;19(12):3016-27. PMID:10856245 doi:10.1093/emboj/19.12.3016

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1erj"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 DOMAIN OF TUP1==
-<StructureSection load='1erj' size='340' side='right' caption='[[1erj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1erj' size='340' side='right'caption='[[1erj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1erj]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ERJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1erj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERJ FirstGlance]. <br>
-</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=1erj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1erj RCSB], [http://www.ebi.ac.uk/pdbsum/1erj PDBsum]</span></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]] 2.3&#8491;</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=1erj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erj OCA], [https://pdbe.org/1erj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erj RCSB], [https://www.ebi.ac.uk/pdbsum/1erj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erj ProSAT]</span></td></tr>
 </table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/1erj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/1erj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1erj ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 23: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1erj" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Johnson, A D]]
+[[Category: Johnson AD]]
-[[Category: Redd, M J]]
+[[Category: Redd MJ]]
-[[Category: Sprague, E R]]
+[[Category: Sprague ER]]
-[[Category: Wolberger, C]]
+[[Category: Wolberger C]]
-[[Category: Beta-propeller]]
-[[Category: Transcription inhibitor]]

1erj

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 DOMAIN OF TUP1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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