Back to Search
Start Over
BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2023 Sep 22; Vol. 51 (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.<br /> (© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 51
- Issue :
- 17
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 37503837
- Full Text :
- https://doi.org/10.1093/nar/gkad613