|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==SOLUTION STRUCTURE OF THE CLR4 CHROMO DOMAIN== | | ==SOLUTION STRUCTURE OF THE CLR4 CHROMO DOMAIN== |
| - | <StructureSection load='1g6z' size='340' side='right'caption='[[1g6z]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | + | <StructureSection load='1g6z' size='340' side='right'caption='[[1g6z]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G6Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G6Z FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLR4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1g6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6z OCA], [https://pdbe.org/1g6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g6z RCSB], [https://www.ebi.ac.uk/pdbsum/1g6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6z 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=1g6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6z OCA], [https://pdbe.org/1g6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g6z RCSB], [https://www.ebi.ac.uk/pdbsum/1g6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CLR4_SCHPO CLR4_SCHPO]] Histone methyltransferase. Catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.<ref>PMID:16024659</ref> <ref>PMID:8138176</ref>
| + | [https://www.uniprot.org/uniprot/CLR4_SCHPO CLR4_SCHPO] Histone methyltransferase. Catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.<ref>PMID:16024659</ref> <ref>PMID:8138176</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 356]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altieri, A S]] | + | [[Category: Schizosaccharomyces pombe]] |
| - | [[Category: Byrd, R A]] | + | [[Category: Altieri AS]] |
| - | [[Category: Horita, D A]] | + | [[Category: Byrd RA]] |
| - | [[Category: Ivanova, A V]] | + | [[Category: Horita DA]] |
| - | [[Category: Klar, A J]] | + | [[Category: Ivanova AV]] |
| - | [[Category: Transferase]] | + | [[Category: Klar AJ]] |
| Structural highlights
Function
CLR4_SCHPO Histone methyltransferase. Catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.[1] [2]
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 encapsulation of otherwise transcribable loci within transcriptionally inactive heterochromatin is rapidly gaining recognition as an important mechanism of epigenetic gene regulation. In the fission yeast Schizosaccharomyces pombe, heterochromatinization of the mat2/mat3 loci silences the mating-type information encoded within these loci. Here, we present the solution structure of the chromo domain from the cryptic loci regulator protein Clr4. Clr4 is known to regulate silencing and switching at the mating-type loci and to affect chromatin structure at centromeres. Clr4 and its human and Drosophila homologs have been identified as histone H3-specific methyltransferases, further implicating this family of proteins in chromatin remodeling. Our structure highlights a conserved surface that may be involved in chromo domain-ligand interactions. We have also analyzed two chromo domain mutants (W31G and W41G) that previously were shown to affect silencing and switching in full-length Clr4. Both mutants are significantly destabilized relative to wild-type.
Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4.,Horita DA, Ivanova AV, Altieri AS, Klar AJ, Byrd RA J Mol Biol. 2001 Mar 30;307(3):861-70. PMID:11273706[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horn PJ, Bastie JN, Peterson CL. A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation. Genes Dev. 2005 Jul 15;19(14):1705-14. PMID:16024659 doi:http://dx.doi.org/10.1101/gad.1328005
- ↑ Ekwall K, Ruusala T. Mutations in rik1, clr2, clr3 and clr4 genes asymmetrically derepress the silent mating-type loci in fission yeast. Genetics. 1994 Jan;136(1):53-64. PMID:8138176
- ↑ Horita DA, Ivanova AV, Altieri AS, Klar AJ, Byrd RA. Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4. J Mol Biol. 2001 Mar 30;307(3):861-70. PMID:11273706 doi:10.1006/jmbi.2001.4515
|
