6NZ2
NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae
Summary for 6NZ2
| Entry DOI | 10.2210/pdb6nz2/pdb |
| NMR Information | BMRB: 30570 |
| Descriptor | Box C/D snoRNA protein 1 (1 entity in total) |
| Functional Keywords | snornp assembly, rna binding, rna binding protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 21864.26 |
| Authors | Bragantini, B.,Quinternet, M.,Charpentier, B.,Manival, X. (deposition date: 2019-02-12, release date: 2020-08-19, Last modification date: 2024-05-15) |
| Primary citation | Bragantini, B.,Charron, C.,Bourguet, M.,Paul, A.,Tiotiu, D.,Rothe, B.,Marty, H.,Terral, G.,Hessmann, S.,Decourty, L.,Chagot, M.E.,Strub, J.M.,Massenet, S.,Bertrand, E.,Quinternet, M.,Saveanu, C.,Cianferani, S.,Labialle, S.,Manival, X.,Charpentier, B. The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity. Nat Commun, 12:1859-1859, 2021 Cited by PubMed Abstract: 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. PubMed: 33767140DOI: 10.1038/s41467-021-22077-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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