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| | ==Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1== | | ==Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1== |
| - | <StructureSection load='5ikf' size='340' side='right' caption='[[5ikf]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5ikf' size='340' side='right'caption='[[5ikf]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ikf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ikf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IKF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mit1, SPBP35G2.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), clr1, SPBC2D10.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5ikf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikf OCA], [http://pdbe.org/5ikf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ikf RCSB], [http://www.ebi.ac.uk/pdbsum/5ikf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikf 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=5ikf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikf OCA], [https://pdbe.org/5ikf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ikf RCSB], [https://www.ebi.ac.uk/pdbsum/5ikf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MIT1_SCHPO MIT1_SCHPO]] Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).<ref>PMID:17289569</ref> [[http://www.uniprot.org/uniprot/CLR1_SCHPO CLR1_SCHPO]] Regulates silencing of the mat2 and mat3 loci. Organizes the chromatin structure of the mating-type region where it also participates in establishing the 'cold spot' for recombination. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).<ref>PMID:1644273</ref> <ref>PMID:17289569</ref> | + | [https://www.uniprot.org/uniprot/MIT1_SCHPO MIT1_SCHPO] Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).<ref>PMID:17289569</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Brugger, C]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Schalch, T]]
| + | [[Category: Brugger C]] |
| - | [[Category: Alpha-helical]]
| + | [[Category: Schalch T]] |
| - | [[Category: Complex]] | + | |
| - | [[Category: Protein-protein interface]] | + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
MIT1_SCHPO Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).[1]
Publication Abstract from PubMed
Nucleosome remodeling and deacetylation (NuRD) complexes are co-transcriptional regulators implicated in differentiation, development, and diseases. Methyl-CpG binding domain (MBD) proteins play an essential role in recruitment of NuRD complexes to their target sites in chromatin. The related SHREC complex in fission yeast drives transcriptional gene silencing in heterochromatin through cooperation with HP1 proteins. How remodeler and histone deacetylase (HDAC) cooperate within NuRD complexes remains unresolved. We determined that in SHREC the two modules occupy distant sites on the scaffold protein Clr1 and that repressive activity of SHREC can be modulated by the expression level of the HDAC-associated Clr1 domain alone. Moreover, the crystal structure of Clr2 reveals an MBD-like domain mediating recruitment of the HDAC module to heterochromatin. Thus, SHREC bi-functionality is organized in two separate modules with separate recruitment mechanisms, which work together to elicit transcriptional silencing at heterochromatic loci.
SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules.,Job G, Brugger C, Xu T, Lowe BR, Pfister Y, Qu C, Shanker S, Banos Sanz JI, Partridge JF, Schalch T Mol Cell. 2016 Apr 21;62(2):207-21. doi: 10.1016/j.molcel.2016.03.016. PMID:27105116[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sugiyama T, Cam HP, Sugiyama R, Noma K, Zofall M, Kobayashi R, Grewal SI. SHREC, an effector complex for heterochromatic transcriptional silencing. Cell. 2007 Feb 9;128(3):491-504. PMID:17289569 doi:http://dx.doi.org/10.1016/j.cell.2006.12.035
- ↑ Job G, Brugger C, Xu T, Lowe BR, Pfister Y, Qu C, Shanker S, Banos Sanz JI, Partridge JF, Schalch T. SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules. Mol Cell. 2016 Apr 21;62(2):207-21. doi: 10.1016/j.molcel.2016.03.016. PMID:27105116 doi:http://dx.doi.org/10.1016/j.molcel.2016.03.016
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