1sse

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(New page: 200px<br /><applet load="1sse" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sse" /> '''Solution structure of the oxidized form of t...)
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[[Image:1sse.gif|left|200px]]<br /><applet load="1sse" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sse" />
 
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'''Solution structure of the oxidized form of the Yap1 redox domain'''<br />
 
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==Overview==
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==Solution structure of the oxidized form of the Yap1 redox domain==
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The ability of organisms to alter their gene expression patterns in, response to environmental changes is essential for viability. A central, regulator of the response to oxidative stress in Saccharomyces cerevisiae, is the Yap1 transcription factor. Upon activation by increased levels of, reactive oxygen species, Yap1 rapidly redistributes to the nucleus where, it regulates the expression of up to 70 genes. Here we identify a, redox-regulated domain of Yap1 and determine its high-resolution solution, structure. In the active oxidized form, a nuclear export signal (NES) in, the carboxy-terminal cysteine-rich domain is masked by, disulphide-bond-mediated interactions with a conserved amino-terminal, alpha-helix. Point mutations that weaken the hydrophobic interactions, between the N-terminal alpha-helix and the C-terminal NES-containing, domain abolished redox-regulated changes in subcellular localization of, Yap1. Upon reduction of the disulphide bonds, Yap1 undergoes a change to, an unstructured conformation that exposes the NES and allows, redistribution to the cytoplasm. These results reveal the structural basis, of redox-dependent Yap1 localization and provide a previously unknown, mechanism of transcription factor regulation by reversible intramolecular, disulphide bond formation.
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<StructureSection load='1sse' size='340' side='right'caption='[[1sse]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sse]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SSE FirstGlance]. <br>
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1SSE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SSE OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sse OCA], [https://pdbe.org/1sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sse RCSB], [https://www.ebi.ac.uk/pdbsum/1sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sse ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structural basis for redox regulation of Yap1 transcription factor localization., Wood MJ, Storz G, Tjandra N, Nature. 2004 Aug 19;430(7002):917-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15318225 15318225]
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== Function ==
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[[Category: Protein complex]]
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[https://www.uniprot.org/uniprot/AP1_YEAST AP1_YEAST] Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Activation by hydrogen peroxide or thiol-reactive chemicals elicit distinct adaptive gene responses. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.<ref>PMID:10347154</ref> <ref>PMID:11013218</ref> <ref>PMID:11274141</ref> <ref>PMID:11509657</ref> <ref>PMID:12006656</ref> <ref>PMID:12437921</ref> <ref>PMID:12582119</ref> <ref>PMID:12743123</ref> <ref>PMID:14556629</ref> <ref>PMID:14556853</ref> <ref>PMID:1525853</ref> <ref>PMID:20971184</ref> <ref>PMID:8182076</ref> <ref>PMID:9065458</ref> <ref>PMID:9372930</ref> <ref>PMID:9469820</ref> <ref>PMID:9857197</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ss/1sse_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1sse ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Storz, G.]]
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[[Category: Storz G]]
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[[Category: Tjandra, N.]]
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[[Category: Tjandra N]]
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[[Category: Wood, M.J.]]
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[[Category: Wood MJ]]
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[[Category: disulfide bond]]
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[[Category: nes]]
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[[Category: nuclear export signal]]
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[[Category: redox-regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:37:35 2007''
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Current revision

Solution structure of the oxidized form of the Yap1 redox domain

PDB ID 1sse

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