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| | <StructureSection load='2r0s' size='340' side='right'caption='[[2r0s]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2r0s' size='340' side='right'caption='[[2r0s]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2r0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2r0s]] is a 1 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=2R0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0S FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r0v|2r0v]], [[2r0y|2r0y]], [[2r10|2r10]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RSC4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2r0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0s OCA], [https://pdbe.org/2r0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0s RCSB], [https://www.ebi.ac.uk/pdbsum/2r0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0s 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=2r0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0s OCA], [https://pdbe.org/2r0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0s RCSB], [https://www.ebi.ac.uk/pdbsum/2r0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RSC4_YEAST RSC4_YEAST]] Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.<ref>PMID:8980231</ref> <ref>PMID:10025404</ref> <ref>PMID:10329629</ref> <ref>PMID:12183366</ref> <ref>PMID:12072455</ref> <ref>PMID:12697820</ref>
| + | [https://www.uniprot.org/uniprot/RSC4_YEAST RSC4_YEAST] Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.<ref>PMID:8980231</ref> <ref>PMID:10025404</ref> <ref>PMID:10329629</ref> <ref>PMID:12183366</ref> <ref>PMID:12072455</ref> <ref>PMID:12697820</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/2r0s_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/2r0s_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cairns, B R]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Ferris, E]] | + | [[Category: Cairns BR]] |
| - | [[Category: Heroux, A]] | + | [[Category: Ferris E]] |
| - | [[Category: Hill, C P]] | + | [[Category: Heroux A]] |
| - | [[Category: Kasten, M M]] | + | [[Category: Hill CP]] |
| - | [[Category: VanDemark, A P]] | + | [[Category: Kasten MM]] |
| - | [[Category: Acetylation]]
| + | [[Category: VanDemark AP]] |
| - | [[Category: Bromodomain]]
| + | |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Chromatin regulator]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Remodeler]]
| + | |
| - | [[Category: Rsc]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
RSC4_YEAST Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.[1] [2] [3] [4] [5] [6]
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
An important issue for chromatin remodeling complexes is how their bromodomains recognize particular acetylated lysine residues in histones. The Rsc4 subunit of the yeast remodeler RSC contains an essential tandem bromodomain (TBD) that binds acetylated K14 of histone H3 (H3K14ac). We report a series of crystal structures that reveal a compact TBD that binds H3K14ac in the second bromodomain and, remarkably, binds acetylated K25 of Rsc4 itself in the first bromodomain. Endogenous Rsc4 is acetylated only at K25, and Gcn5 is identified as necessary and sufficient for Rsc4 K25 acetylation in vivo and in vitro. Rsc4 K25 acetylation inhibits binding to H3K14ac, and mutation of Rsc4 K25 results in altered growth rates. These data suggest an autoregulatory mechanism in which Gcn5 performs both the activating (H3K14ac) and inhibitory (Rsc4 K25ac) modifications, perhaps to provide temporal regulation. Additional regulatory mechanisms are indicated as H3S10 phosphorylation inhibits Rsc4 binding to H3K14ac peptides.
Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation.,VanDemark AP, Kasten MM, Ferris E, Heroux A, Hill CP, Cairns BR Mol Cell. 2007 Sep 7;27(5):817-28. PMID:17803945[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cairns BR, Lorch Y, Li Y, Zhang M, Lacomis L, Erdjument-Bromage H, Tempst P, Du J, Laurent B, Kornberg RD. RSC, an essential, abundant chromatin-remodeling complex. Cell. 1996 Dec 27;87(7):1249-60. PMID:8980231
- ↑ Lorch Y, Zhang M, Kornberg RD. Histone octamer transfer by a chromatin-remodeling complex. Cell. 1999 Feb 5;96(3):389-92. PMID:10025404
- ↑ Moreira JM, Holmberg S. Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC. EMBO J. 1999 May 17;18(10):2836-44. PMID:10329629 doi:10.1093/emboj/18.10.2836
- ↑ Saha A, Wittmeyer J, Cairns BR. Chromatin remodeling by RSC involves ATP-dependent DNA translocation. Genes Dev. 2002 Aug 15;16(16):2120-34. PMID:12183366 doi:10.1101/gad.995002
- ↑ Chai B, Hsu JM, Du J, Laurent BC. Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway. Genetics. 2002 Jun;161(2):575-84. PMID:12072455
- ↑ Hsu JM, Huang J, Meluh PB, Laurent BC. The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation. Mol Cell Biol. 2003 May;23(9):3202-15. PMID:12697820
- ↑ VanDemark AP, Kasten MM, Ferris E, Heroux A, Hill CP, Cairns BR. Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation. Mol Cell. 2007 Sep 7;27(5):817-28. PMID:17803945 doi:http://dx.doi.org/10.1016/j.molcel.2007.08.018
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