A newly discovered function for RNase L in regulating translation termination.
Nat Struct Mol Biol
; 12(6): 505-12, 2005 Jun.
Article
em En
| MEDLINE
| ID: mdl-15908960
ABSTRACT
The antiviral and antiproliferative effects of interferons are mediated in part by the 2'-5' oligoadenylate-RNase L RNA decay pathway. RNase L is an endoribonuclease that requires 2'-5' oligoadenylates to cleave single-stranded RNA. In this report we present evidence demonstrating a role for RNase L in translation. We identify and characterize the human translation termination factor eRF3/GSPT1 as an interacting partner of RNase L. We show that interaction of eRF3 with RNase L leads to both increased translation readthrough efficiency at premature termination codons and increased +1 frameshift efficiency at the antizyme +1 frameshift site. On the basis of our results, we present a model describing how RNase L is involved in regulating gene expression by modulating the translation termination process.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Terminação Traducional da Cadeia Peptídica
/
Fatores de Terminação de Peptídeos
/
Endorribonucleases
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Nat Struct Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Estados Unidos