6thl

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Current revision (13:02, 24 January 2024) (edit) (undo)
 
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==Crystal structure of the complex between RTT106 and BCD1==
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<StructureSection load='6thl' size='340' side='right'caption='[[6thl]]' scene=''>
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<StructureSection load='6thl' size='340' side='right'caption='[[6thl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6thl]] is a 2 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=6THL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THL FirstGlance]. <br>
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</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=6thl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thl OCA], [https://pdbe.org/6thl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6thl RCSB], [https://www.ebi.ac.uk/pdbsum/6thl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6thl ProSAT]</span></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]] 2.8&#8491;</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=6thl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thl OCA], [https://pdbe.org/6thl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6thl RCSB], [https://www.ebi.ac.uk/pdbsum/6thl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6thl ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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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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Biogenesis of eukaryotic box C/D small nucleolar ribonucleoproteins initiates co-transcriptionally and requires the action of the assembly machinery including the Hsp90/R2TP complex, the Rsa1p:Hit1p heterodimer and the Bcd1 protein. We present genetic interactions between the Rsa1p-encoding gene and genes involved in chromatin organization including RTT106 that codes for the H3-H4 histone chaperone Rtt106p controlling H3K56ac deposition. We show that Bcd1p binds Rtt106p and controls its transcription-dependent recruitment by reducing its association with RNA polymerase II, modulating H3K56ac levels at gene body. We reveal the 3D structures of the free and Rtt106p-bound forms of Bcd1p using nuclear magnetic resonance and X-ray crystallography. The interaction is also studied by a combination of biophysical and proteomic techniques. Bcd1p interacts with a region that is distinct from the interaction interface between the histone chaperone and histone H3. Our results are evidence for a protein interaction interface for Rtt106p that controls its transcription-associated activity.
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The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity.,Bragantini B, Charron C, Bourguet M, Paul A, Tiotiu D, Rothe B, Marty H, Terral G, Hessmann S, Decourty L, Chagot ME, Strub JM, Massenet S, Bertrand E, Quinternet M, Saveanu C, Cianferani S, Labialle S, Manival X, Charpentier B Nat Commun. 2021 Mar 25;12(1):1859. doi: 10.1038/s41467-021-22077-4. PMID:33767140<ref>PMID:33767140</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 6thl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Bragantini B]]
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[[Category: Charpentier B]]
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[[Category: Charron C]]
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[[Category: Manival X]]

Current revision

Crystal structure of the complex between RTT106 and BCD1

PDB ID 6thl

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