The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity.
Cell Proliferation
/ physiology
Chromatin
/ genetics
Chromatin Assembly and Disassembly
/ genetics
Crystallography, X-Ray
Histones
/ metabolism
Molecular Chaperones
/ metabolism
Nuclear Magnetic Resonance, Biomolecular
RNA Polymerase II
/ metabolism
RNA-Binding Proteins
/ metabolism
Ribonucleoproteins, Small Nucleolar
/ genetics
Ribosomal Proteins
/ genetics
Ribosomes
/ metabolism
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ genetics
Transcription, Genetic
/ genetics
Transcriptional Activation
/ physiology
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
25 03 2021
25 03 2021
Historique:
received:
17
12
2019
accepted:
26
02
2021
entrez:
26
3
2021
pubmed:
27
3
2021
medline:
10
4
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33767140
doi: 10.1038/s41467-021-22077-4
pii: 10.1038/s41467-021-22077-4
pmc: PMC7994586
doi:
Substances chimiques
Bcd1 protein, S cerevisiae
0
Chromatin
0
Histones
0
Molecular Chaperones
0
RNA-Binding Proteins
0
RSA1 protein, S cerevisiae
0
Ribonucleoproteins, Small Nucleolar
0
Ribosomal Proteins
0
Rtt106 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
RNA Polymerase II
EC 2.7.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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