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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| Main Authors: | , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
22 November 2022
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| In: |
Cell reports
Year: 2022, Volume: 41, Issue: 8, Pages: 1-22 |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2022.111684 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.celrep.2022.111684 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S2211124722015583 
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| Author Notes: | Benjamin Lau, Olga Beine-Golovchuk, Markus Kornprobst, Jingdong Cheng, Dieter Kressler, Beáta Jády, Tamás Kiss, Roland Beckmann, Ed Hurt |
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| 520 | |a 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. | ||
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