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

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)9369-9384
Number of pages16
JournalNucleic acids research
Volume51
Issue number17
Early online date28 Jul 2023
DOIs
StatePublished - 22 Sep 2023

All Science Journal Classification (ASJC) codes

  • Genetics

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