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Lookup NU author(s): Dr Nick Watkins
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2021, The Author(s).Synthesis of eukaryotic ribosomes involves the assembly and maturation of precursor particles (pre-ribosomal particles) containing ribosomal RNA (rRNA) precursors, ribosomal proteins (RPs) and a plethora of assembly factors (AFs). Formation of the earliest precursors of the 60S ribosomal subunit (pre-60S r-particle) is among the least understood stages of ribosome biogenesis. It involves the Npa1 complex, a protein module suggested to play a key role in the early structuring of the pre-rRNA. Npa1 displays genetic interactions with the DExD-box protein Dbp7 and interacts physically with the snR190 box C/D snoRNA. We show here that snR190 functions as a snoRNA chaperone, which likely cooperates with the Npa1 complex to initiate compaction of the pre-rRNA in early pre-60S r-particles. We further show that Dbp7 regulates the dynamic base-pairing between snR190 and the pre-rRNA within the earliest pre-60S r-particles, thereby participating in structuring the peptidyl transferase center (PTC) of the large ribosomal subunit.
Author(s): Jaafar M, Contreras J, Dominique C, Martin-Villanueva S, Capeyrou R, Vitali P, Rodriguez-Galan O, Velasco C, Humbert O, Watkins NJ, Villalobo E, Bohnsack KE, Bohnsack MT, Henry Y, Merhi RA, de la Cruz J, Henras AK
Publication type: Article
Publication status: Published
Journal: Nature Communications
Print publication date: 01/12/2021
Online publication date: 22/11/2021
Acceptance date: 22/09/2021
Date deposited: 03/11/2021
ISSN (electronic): 2041-1723
Publisher: Nature Research
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