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Angiogenin-induced tRNA-derived stress-induced RNAs promote stress-induced stress granule assembly.


ABSTRACT: Angiogenin (ANG) is a secreted ribonuclease that cleaves tRNA to initiate a stress-response program in mammalian cells. Here we show that ANG inhibits protein synthesis and promotes arsenite- and pateamine A-induced assembly of stress granules (SGs). These effects are abrogated in cells transfected with the ANG inhibitor RNH1. Transfection of natural or synthetic 5'- but not 3'-tRNA fragments (tRNA-derived stress-induced RNAs; tiRNAs) induces the phospho-eukaryotic translation initiation factor 2alpha-independent assembly of SGs. Natural 5'-tiRNAs but not 3'-tiRNAs are capped with a 5'-monophosphate that is required for optimal SG assembly. These findings reveal that SG assembly is a component of the ANG- and tiRNA-induced stress response program.

SUBMITTER: Emara MM 

PROVIDER: S-EPMC2856301 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Angiogenin-induced tRNA-derived stress-induced RNAs promote stress-induced stress granule assembly.

Emara Mohamed M MM   Ivanov Pavel P   Hickman Tyler T   Dawra Nemisha N   Tisdale Sarah S   Kedersha Nancy N   Hu Guo-Fu GF   Anderson Paul P  

The Journal of biological chemistry 20100203 14


Angiogenin (ANG) is a secreted ribonuclease that cleaves tRNA to initiate a stress-response program in mammalian cells. Here we show that ANG inhibits protein synthesis and promotes arsenite- and pateamine A-induced assembly of stress granules (SGs). These effects are abrogated in cells transfected with the ANG inhibitor RNH1. Transfection of natural or synthetic 5'- but not 3'-tRNA fragments (tRNA-derived stress-induced RNAs; tiRNAs) induces the phospho-eukaryotic translation initiation factor  ...[more]

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