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Angiogenin-induced tRNA fragments inhibit translation initiation.

Abstract：

:Angiogenin is a stress-activated ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs). Transfection of natural or synthetic tiRNAs inhibits protein synthesis and triggers the phospho-eIF2α-independent assembly of stress granules (SGs), essential components of the stress response program. We show that selected tiRNAs inhibit protein synthesis by displacing eIF4G/eIF4A from uncapped > capped RNAs. tiRNAs also displace eIF4F, but not eIF4E:4EBP1, from isolated m(7)G cap. We identify a terminal oligoguanine motif that is required to displace the eIF4F complex, inhibit translation, and induce SG assembly. We show that the tiRNA-associated translational silencer YB-1 contributes to angiogenin-, tiRNA-, and oxidative stress-induced translational repression. Our data reveal some of the mechanisms by which stress-induced tRNA cleavage inhibits protein synthesis and activates a cytoprotective stress response program.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Ivanov P,Emara MM,Villen J,Gygi SP,Anderson P

doi

10.1016/j.molcel.2011.06.022

subject

Has Abstract

pub_date

2011-08-19 00:00:00

pages

613-23

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(11)00524-7

journal_volume

43

pub_type

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