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

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 suppres...

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Bibliographic Details
Published in:Cell reports (Cambridge) 2022-11, Vol.41 (8), p.111684-111684, Article 111684
Main Authors: Lau, Benjamin, Beine-Golovchuk, Olga, Kornprobst, Markus, Cheng, Jingdong, Kressler, Dieter, Jády, Beáta, Kiss, Tamás, Beckmann, Roland, Hurt, Ed
Format: Article
Language:English
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Summary: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.
ISSN:2211-1247
2211-1247
DOI:10.1016/j.celrep.2022.111684