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BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures
- Source :
- Danino , Y M , Molitor , L , Rosenbaum-Cohen , T , Kaiser , S , Cohen , Y , Porat , Z , Marmor-Kollet , H , Katina , C , Savidor , A , Rotkopf , R , Ben-Isaac , E , Golani , O , Levin , Y , Monchaud , D , Hickson , I D & Hornstein , E 2023 , ' BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures ' , Nucleic Acids Research , vol. 51 , no. 17 , pp. 9369-9384 .
- Publication Year :
- 2023
-
Abstract
- Bloom's syndrome (BLM) protein is a known nuclear helicase that is able to unwind DNA secondary structures such as G-quadruplexes (G4s). However, its role in the regulation of cytoplasmic processes that involve RNA G-quadruplexes (rG4s) has not been previously studied. Here, we demonstrate that BLM is recruited to stress granules (SGs), which are cytoplasmic biomolecular condensates composed of RNAs and RNA-binding proteins. BLM is enriched in SGs upon different stress conditions and in an rG4-dependent manner. Also, we show that BLM unwinds rG4s and acts as a negative regulator of SG formation. Altogether, our data expand the cellular activity of BLM and shed light on the function that helicases play in the dynamics of biomolecular condensates.
Details
- Database :
- OAIster
- Journal :
- Danino , Y M , Molitor , L , Rosenbaum-Cohen , T , Kaiser , S , Cohen , Y , Porat , Z , Marmor-Kollet , H , Katina , C , Savidor , A , Rotkopf , R , Ben-Isaac , E , Golani , O , Levin , Y , Monchaud , D , Hickson , I D & Hornstein , E 2023 , ' BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures ' , Nucleic Acids Research , vol. 51 , no. 17 , pp. 9369-9384 .
- Notes :
- application/pdf, English
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1439549940
- Document Type :
- Electronic Resource