Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast

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Jaafar, Mariam | Contreras, Julia | Dominique, Carine | Martín-Villanueva, Sara | Capeyrou, Régine | Vitali, Patrice | Rodríguez-Galán, Olga | Velasco, Carmen | Humbert, Odile | Watkins, Nicholas | Villalobo, Eduardo | Bohnsack, Katherine | Bohnsack, Markus | Henry, Yves | Merhi, Raghida Abou | de la Cruz, Jesús | Henras, Anthony

Edité par CCSD ; Nature Publishing Group -

International audience. 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.

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