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H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation – Dataset 3

ABSTRACT: Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.

INSTRUMENT(S):

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

SUBMITTER: Paulina Fischer

LAB HEAD: Ed Hurt

PROVIDER: PXD054034 | Pride | 2025-05-22

REPOSITORIES: Pride

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H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation – Dataset 1

Project description:Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.

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

Project description: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.

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