%0 Journal Article
%A Jaafar, Mariam
%A Contreras, Julia
%A Dominique, Carine
%A Martín-Villanueva, Sara
%A Capeyrou, Regine
%A Vitali, Patrice
%A Rodriguez-Galan, Olga
%A Velasco, Carmen
%A Humbert, Odile
%A Watkins, Nicholas J
%A Villalobo, Eduardo
%A Bohnsack, Katherine E
%A Bohnsack, Markus T
%A Henry, Yves
%A Merhi, Raghida Abou
%A de-la-Cruz, Jesus
%A Henras, Anthony K
%T Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast.
%D 2021
%U https://hdl.handle.net/10668/27566
%X 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.
%K RNA
%K RNA folding
%K Small RNAs
%~