Tudor-SN and ADAR1 are components of cytoplasmic stress granules
| Autor: | Rebekka Weissbach, A. D. J. Scadden |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Xanthine Oxidase
SND1 Adenosine Deaminase Arsenites viruses Biology Cytoplasmic Granules Article Stress granule Stress Physiological Transcription (biology) RNA interference Cell Line Tumor Humans Molecular Biology Nuclear Proteins RNA-Binding Proteins RNA Transfection Endonucleases Protein Structure Tertiary Cell biology Protein Transport RNA silencing Poly I-C RNA splicing HeLa Cells Protein Binding |
| Zdroj: | RNA. 18:462-471 |
| ISSN: | 1469-9001 1355-8382 |
| DOI: | 10.1261/rna.027656.111 |
| Popis: | Hyperediting by adenosine deaminases that acts on RNA (ADARs) may result in numerous Adenosine-to-Inosine (A-to-I) substitutions within long dsRNA. However, while countless RNAs may undergo hyperediting, the role for inosine-containing hyperedited dsRNA (IU-dsRNA) in cells is poorly understood. We have previously shown that IU-dsRNA binds specifically to various components of cytoplasmic stress granules, as well as to other proteins such as Tudor Staphylococcal Nuclease (Tudor-SN). Tudor-SN has been implicated in diverse roles in mammalian cells, including transcription, splicing, RNAi, and degradation. Moreover, we have shown that Tudor-SN interacts directly with stress granule proteins. Here we show that Tudor-SN localizes to cytoplasmic stress granules in HeLa cells undergoing arsenite-induced oxidative stress, or following transfection with long dsRNA (poly[IC]), which initiates an interferon cascade. We additionally demonstrate a novel interaction between Tudor-SN and ADAR1. Finally, we show that ADAR1 is also localized to stress granules in HeLa cells following various stresses. |
| Databáze: | OpenAIRE |
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