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

Lau, Benjamin H.S.; Beine-Golovchuk, Olga; Kornprobst, Markus; Cheng, Jingdong; Kressler, Dieter; Jády, Beáta E.; Kiss, Tamás; Beckmann, Roland; Hurt, Ed

doi:10.1016/j.celrep.2022.111684

Cited by 1 publication

(2 citation statements)

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“…In order to confirm this conclusion, we analysed the snoRNA composition of the Efg1 purified particle in more detail. For comparison, we had chosen the late factor Kre33 and the early factor Cms1, that is involved in maturation of the 3′ rRNA domain ( 46 ). Consistently, Cms1 was strongly enriched in the Efg1 purification, but reduced in the Kre33 purified 90S particle (Figure 3C ).…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, Cms1 and Efg1 copurified significant amounts of the CD box snoRNAs U3 and U14 as well as the H/ACA snoRNAs snR30 and snR83. However, the amount of coisolated snoRNA differed dramatically: Cms1 coprecipitated predominantly the snoRNA snR83, which is required for optimal maturation of the 3′ domain of early 90S intermediates ( 46 ), whereas the Efg1 eluate contained a high level of the U14 snoRNA (Figure 4B , C).…”

Section: Resultsmentioning

confidence: 99%

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The Efg1–Bud22 dimer associates with the U14 snoRNP contacting the 5′ rRNA domain of an early 90S pre-ribosomal particle

Beine-Golovchuk,

Kallas,

Kunze

et al. 2023

Nucleic Acids Research

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The DEAD-box helicase Dbp4 plays an essential role during the early assembly of the 40S ribosome, which is only poorly understood to date. By applying the yeast two-hybrid method and biochemical approaches, we discovered that Dbp4 interacts with the Efg1–Bud22 dimer. Both factors associate with early pre-90S particles and smaller complexes, each characterized by a high presence of the U14 snoRNA. A crosslink analysis of Bud22 revealed its contact to the U14 snoRNA and the 5′ domain of the nascent 18S rRNA, close to its U14 snoRNA hybridization site. Moreover, depletion of Bud22 or Efg1 specifically affects U14 snoRNA association with pre-ribosomal complexes. Accordingly, we concluded that the role of the Efg1–Bud22 dimer is linked to the U14 snoRNA function on early 90S ribosome intermediates chaperoning the 5′ domain of the nascent 18S rRNA. The successful rRNA folding of the 5′ domain and the release of Efg1, Bud22, Dpb4, U14 snoRNA and associated snoRNP factors allows the subsequent recruitment of the Kre33-Bfr2-Enp2-Lcp5 module towards the 90S pre-ribosome.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%