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2r10

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Revision as of 07:40, 25 October 2017

Structure of an acetylated Rsc4 tandem bromodomain Histone Chimera

Structural highlights

2r10 is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2r0s, 2r0v, 2r0y
Gene:	RSC4 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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/2r10"

@@ Line 1: / Line 1: @@
 ==Structure of an acetylated Rsc4 tandem bromodomain Histone Chimera==
 <StructureSection load='2r10' size='340' side='right' caption='[[2r10]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r0s|2r0s]], [[2r0v|2r0v]], [[2r0y|2r0y]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RSC4 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r10 OCA], [http://pdbe.org/2r10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r10 RCSB], [http://www.ebi.ac.uk/pdbsum/2r10 PDBsum]</span></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=2r10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r10 OCA], [http://pdbe.org/2r10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r10 RCSB], [http://www.ebi.ac.uk/pdbsum/2r10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r10 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 41: / Line 42: @@
 [[Category: Kasten, M M]]
 [[Category: VanDemark, A P]]
+[[Category: Acetylation]]
 [[Category: Bromodomain]]
 [[Category: Chromatin]]

2r10

From Proteopedia

Revision as of 07:40, 25 October 2017

Structure of an acetylated Rsc4 tandem bromodomain Histone Chimera

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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