BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures.

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.

• Authors: Yehuda M Danino, Lena Molitor, Tamar Rosenbaum-Cohen, Sebastian Kaiser, Yahel Cohen, Ziv Porat, Hagai Marmor-Kollet, Corine Katina, Alon Savidor, Ron Rotkopf, Eyal Ben-Isaac, Ofra Golani, Yishai Levin, David Monchaud, Ian D Hickson, Eran Hornstein
• Journal: Nucleic acids research (Nucleic Acids Res) Vol. 51 Issue 17 Pg. 9369-9384 (09 22 2023) ISSN: 1362-4962 [Electronic] England
• PMID: 37503837 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

Chemical References

• DNA
• RecQ Helicases
• RNA
• Bloom syndrome protein

Topics

• Humans
• DNA (chemistry)
• G-Quadruplexes
• RecQ Helicases (metabolism)
• RNA (genetics)
• Stress Granules (metabolism)