Ribosome-bound Upf1 forms distinct 80S complexes and conducts mRNA surveillance.
RNA
; 28(12): 1621-1642, 2022 12.
Article
em En
| MEDLINE
| ID: mdl-36192133
ABSTRACT
Upf1, Upf2, and Upf3, the central regulators of nonsense-mediated mRNA decay (NMD), appear to exercise their NMD functions while bound to elongating ribosomes, and evidence for this conclusion is particularly compelling for Upf1. Hence, we used selective profiling of yeast Upf1ribosome association to define that step in greater detail, understand whether the nature of the mRNA being translated influences Upf180S interaction, and elucidate the functions of ribosome-associated Upf1. Our approach has allowed us to clarify the timing and specificity of Upf1 association with translating ribosomes, obtain evidence for a Upf1 mRNA surveillance function that precedes the activation of NMD, identify a unique ribosome state that generates 37-43 nt ribosome footprints whose accumulation is dependent on Upf1's ATPase activity, and demonstrate that a mutated form of Upf1 can interfere with normal translation termination and ribosome release. In addition, our results strongly support the existence of at least two distinct functional Upf1 complexes in the NMD pathway.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
RNA Helicases
/
Degradação do RNAm Mediada por Códon sem Sentido
Tipo de estudo:
Screening_studies
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article