BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures
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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.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Nucleic Acids Research |
| Vol/bind | 51 |
| Udgave nummer | 17 |
| Sider (fra-til) | 9369-9384 |
| Antal sider | 16 |
| ISSN | 0305-1048 |
| DOI | |
| Status | Udgivet - 2023 |
Bibliografisk note
Funding Information:
E.H. is the Mondry Family Professorial Chair and Head of the Andrea L. and Lawrence A. Wolfe Family Center for Research on Neuroimmunology and Neuromodulation; research at the Hornstein laboratory is supported by the CReATe consortium and ALSA; RADALA Foundation; AFM Telethon [20 576]; Weizmann–Brazil Center for Research on Neurodegeneration at Weizmann Institute of Science; Minerva Foundation, with funding from the Federal German Ministry for Education and Research; ISF Legacy Heritage Fund [828/17]; Israel Science Foundation [135/16, 3497/21, 424/22, 425/22, 372/23]; Target ALS; ERA‐Net for Research Programs on Rare Diseases [eRARE FP7] via the Israel Ministry of Health; United States-Israel Binational Science Foundation [2 021 181]; Dr Sydney Brenner and friends; Edward and Janie Moravitz; Yeda‐Sela; Yeda‐CEO; Israel Ministry of Trade and Industry; Y. Leon Benoziyo Institute for Molecular Medicine; Nella and Leon Benoziyo Center for Neurological Diseases; Kekst Family Institute for Medical Genetics; David and Fela Shapell Family Center for Genetic Disorders Research; Crown Human Genome Center; Nathan, Shirley, Philip, and Charlene Vener New Scientist Fund; Julius and Ray Charlestein Foundation; Fraida Foundation; Wolfson Family Charitable Trust; Adelis Foundation; Merck (UK); M. Halphen; the estates of F. Sherr, L. Asseof, and L. Fulop; Goldhirsh-Yellin Foundation; Redhill Foundation–Sam and Jean Rothberg Charitable Trust; Dr Dvora and Haim Teitelbaum Endowment Fund; Supported by a research grant from the Anita James Rosen Foundation; Robert Packard Center for ALS Research at Johns Hopkins; Y.M.D. is funded by a fellowship from the CNRS-WIS center for research of RNA secondary structures; L.M. is supported by the Minerva Foundation; I.D.H. and S.K. were funded by the Danish National Research Foundation [DNRF115].
Publisher Copyright:
© 2023 The Author(s).
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