Dataset Information

Cms1 coordinates stepwise local 90S pre-ribosome assembly with timely snR83 release Table S2

ABSTRACT: Ribosome synthesis begins in the nucleolus with 90S pre-ribosome construction, but little is known about how the many different snoRNAs that modify the pre-rRNA are timely guided to their target sites. Here, we report a role for Cms1 in such a process. Initially, we discover CMS1 as null suppressor of a nop14 mutant impaired in Rrp12–Enp1 factor recruitment to the 90S. Further investigations detect Cms1 at the 18S rRNA 3'-major domain of an early 90S that carries H/ACA snR83, known to guide pseudouridylation at two target sites within the same subdomain. Cms1 co-precipitates with many 90S factors, but Rrp12-Enp1 encircling the 3'-major domain in the mature 90S is decreased. We suggest that Cms1 associates with the 3’-major domain during early 90S biogenesis to restrict premature Rrp12–Enp1 binding, but allows snR83 to timely perform its modification role before the next 90S assembly steps coupled with Cms1 release take place.

INSTRUMENT(S): LTQ

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Benjamin Lau

LAB HEAD: Prof. Dr. Ed Hurt

PROVIDER: PXD037619 | Pride | 2023-03-11

REPOSITORIES: Pride

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Cms1 coordinates stepwise local 90S pre-ribosome assembly with timely snR83 release.

Lau Benjamin B Beine-Golovchuk Olga O Kornprobst Markus M Cheng Jingdong J Kressler Dieter D Jády Beáta B Kiss Tamás T Beckmann Roland R Hurt Ed E

Cell reports 20221101 8

Ribosome synthesis begins in the nucleolus with 90S pre-ribosome construction, but little is known about how the many different snoRNAs that modify the pre-rRNA are timely guided to their target sites. Here, we report a role for Cms1 in such a process. Initially, we discovered CMS1 as a null suppressor of a nop14 mutant impaired in Rrp12-Enp1 factor recruitment to the 90S. Further investigations detected Cms1 at the 18S rRNA 3' major domain of an early 90S that carried H/ACA snR83, which is know ...[more]

PMID: 36417864

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Project description:Transcription of the several hundred of mouse and human Ribosomal RNA (rRNA) genes accounts for the majority of RNA synthesis in the cell nucleus and is the determinant of cytoplasmic ribosome abundance, a key factor in regulating gene expression. The rRNA genes, referred to globally as the rDNA, are clustered as direct repeats at the Nucleolar Organiser Regions, NORs, of several chromosomes, and in many cells the active repeats are transcribed at near saturation levels. The rDNA is also a hotspot of recombination and chromosome breakage, and hence understanding its control has broad importance. Despite the need for a high level of rDNA transcription, typically only a fraction of the rDNA is transcriptionally active, and some NORs are permanently silenced by CpG methylation. Various chromatin-remodelling complexes have been implicated in counteracting silencing to maintain rDNA activity. However, the chromatin structure of the active rDNA fraction is still far from clear. Here we have combined a high-resolution ChIP-Seq protocol with conditional inactivation of key basal factors to better understand what determines active rDNA chromatin. The data resolve questions concerning the interdependence of the basal transcription factors, show that preinitiation complex formation is driven by the architectural factor UBF (UBTF) independently of transcription, and exclude a significant role for termination by a torpedomechanism. They further reveal the existence of an asymmetric Boundary Complex formed by CTCF, Cohesin and three phased nucleosomes lying adjacent to the rDNA Enhancer and an arrested RNA Polymerase I complex. We find that this complex is the only site of active histone modification in the whole 45kbp rDNA repeat. Strikingly, the Enhancer Boundary Complex not only delimits each functional rRNA gene, but also is stably maintained after gene inactivation and the re-establishment of surrounding repressive chromatin. Our data define the poised state of rDNA chromatin and place the Enhancer Boundary Complex as the likely entry point for the chromatin remodelling complexes.

			Action	DRS
	JB-5Ala.raw	Raw
	JB-Wt.raw	Raw
	Oxidation__M_Sites.txt	Txt
	allPeptides.txt	Txt
	allSpectra.CID.ITMS.iso_0.apl	Other