Bragantini, BenoitCharron, ChristopheBourguet, MaximePaul, ArnaudTiotiu, DecebalRothe, BenjaminMarty, HeleneTerral, GuillaumeHessmann, SteveDecourty, LaurenceChagot, Marie-EveStrub, Jean-MarcMassenet, SeverineBertrand, EdouardQuinternet, MarcSaveanu, CosminCianferani, SarahLabialle, StephaneManival, XavierCharpentier, Bruno2021-05-082021-05-082021-05-082021-03-2510.1038/s41467-021-22077-4https://infoscience.epfl.ch/handle/20.500.14299/177973WOS:000637989400010Biogenesis 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. Biogenesis of small nucleolar RNAs ribonucleoproteins (snoRNPs) requires dedicated assembly machinery. Here, the authors show that a subset of snoRNP assembly factors interacts, genetically or directly, with factors modulating chromatin architecture, suggesting a link between ribosome formation and chromatin functions.Multidisciplinary SciencesScience & Technology - Other Topicstext::journal::journal article::research article