Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast.
Nat Commun
; 12(1): 6153, 2021 10 22.
Article
em En
| MEDLINE
| ID: mdl-34686656
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Chaperonas Moleculares
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RNA Nucleolar Pequeno
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Proteínas de Saccharomyces cerevisiae
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RNA Helicases DEAD-box
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Subunidades Ribossômicas Maiores de Eucariotos
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article