6THL

Crystal structure of the complex between RTT106 and BCD1

Summary for 6THL

• Entry DOI: 10.2210/pdb6thl/pdb
• Descriptor: Rtt106p, Box C/D snoRNA protein 1 (2 entities in total)
• Functional Keywords: chaperone, snornp
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 49093.53

Authors

Charron, C.,Bragantini, B.,Manival, X.,Charpentier, B. (deposition date: 2019-11-20, release date: 2020-12-02, Last modification date: 2024-01-24)

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

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: 33767140
DOI: 10.1038/s41467-021-22077-4

Experimental method

X-RAY DIFFRACTION (2.8 Å)