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


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 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 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.

SUBMITTER: Lau B 

PROVIDER: S-EPMC9715914 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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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]

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