3to1

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==Two surfaces on Rtt106 mediate histone binding and chaperone activity==
==Two surfaces on Rtt106 mediate histone binding and chaperone activity==
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<StructureSection load='3to1' size='340' side='right' caption='[[3to1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='3to1' size='340' side='right'caption='[[3to1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3to1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TO1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3to1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TO1 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT106, YNL206C, N1346 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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=3to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to1 OCA], [http://pdbe.org/3to1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3to1 RCSB], [http://www.ebi.ac.uk/pdbsum/3to1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3to1 ProSAT]</span></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=3to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to1 OCA], [https://pdbe.org/3to1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3to1 RCSB], [https://www.ebi.ac.uk/pdbsum/3to1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3to1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RT106_YEAST RT106_YEAST]] Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:16157874</ref> <ref>PMID:17410207</ref> <ref>PMID:19683497</ref> <ref>PMID:20188666</ref> <ref>PMID:21763693</ref> <ref>PMID:22156209</ref> <ref>PMID:21444721</ref> <ref>PMID:21698254</ref> <ref>PMID:21978826</ref> <ref>PMID:22128187</ref> <ref>PMID:20007951</ref>
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[https://www.uniprot.org/uniprot/RT106_YEAST RT106_YEAST] Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:16157874</ref> <ref>PMID:17410207</ref> <ref>PMID:19683497</ref> <ref>PMID:20188666</ref> <ref>PMID:21763693</ref> <ref>PMID:22156209</ref> <ref>PMID:21444721</ref> <ref>PMID:21698254</ref> <ref>PMID:21978826</ref> <ref>PMID:22128187</ref> <ref>PMID:20007951</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The histone chaperone Rtt106 binds histone H3 acetylated at lysine 56 (H3K56ac) and facilitates nucleosome assembly during several molecular processes. Both the structural basis of this modification-specific recognition and how this recognition informs Rtt106 function are presently unclear. Guided by our crystal structure of Rtt106, we identified two regions on its double-pleckstrin homology domain architecture that mediated histone binding. When histone binding was compromised, Rtt106 localized properly to chromatin but failed to deliver H3K56ac, leading to replication and silencing defects. By mutating analogous regions in the structurally homologous chromatin-reorganizer Pob3, we revealed a conserved histone-binding function for a basic patch found on both proteins. In contrast, a loop connecting two beta-strands was required for histone binding by Rtt106 but was dispensable for Pob3 function. Unlike Rtt106, Pob3 histone binding was modification-independent, implicating the loop of Rtt106 in H3K56ac-specific recognition in vivo. Our studies described the structural origins of Rtt106 function, identified a conserved histone-binding surface, and defined a critical role for Rtt106:H3K56ac-binding specificity in silencing and replication-coupled nucleosome turnover.
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Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.,Zunder RM, Antczak AJ, Berger JM, Rine J Proc Natl Acad Sci U S A. 2011 Dec 23. PMID:22198837<ref>PMID:22198837</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3to1" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
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[[Category: Large Structures]]
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[[Category: Antczak, A J]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Berger, J M]]
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[[Category: Antczak AJ]]
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[[Category: Rine, J]]
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[[Category: Berger JM]]
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[[Category: Zunder, R M]]
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[[Category: Rine J]]
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[[Category: Chaperone]]
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[[Category: Zunder RM]]
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[[Category: Histone chaperone]]
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Current revision

Two surfaces on Rtt106 mediate histone binding and chaperone activity

PDB ID 3to1

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