A newly discovered function for RNase L in regulating translation termination.

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.

journal_name

Nat Struct Mol Biol

authors

Le Roy F,Salehzada T,Bisbal C,Dougherty JP,Peltz SW

doi

10.1038/nsmb944

keywords:

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

505-12

issue

6

eissn

1545-9993

issn

1545-9985

pii

nsmb944

journal_volume

12

pub_type

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