6nz2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae== | |
| + | <StructureSection load='6nz2' size='340' side='right'caption='[[6nz2]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6nz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NZ2 FirstGlance]. <br> | ||
| + | </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=6nz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nz2 OCA], [https://pdbe.org/6nz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nz2 RCSB], [https://www.ebi.ac.uk/pdbsum/6nz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nz2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BCD1_YEAST BCD1_YEAST] Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.<ref>PMID:12837249</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6nz2" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Quinternet | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Bragantini B]] | ||
| + | [[Category: Charpentier B]] | ||
| + | [[Category: Manival X]] | ||
| + | [[Category: Quinternet M]] | ||
Current revision
NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae
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