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

doi:10.1093/nar/gkad613

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^*

^*Corresponding author for this work

Molecular Aging Program

Research output: Contribution to journal › Journal article › Research › peer-review

3 Citations (Scopus)

16 Downloads (Pure)

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 language	English
Journal	Nucleic Acids Research
Volume	51
Issue number	17
Pages (from-to)	9369-9384
Number of pages	16
ISSN	0305-1048
DOIs	https://doi.org/10.1093/nar/gkad613
Publication status	Published - 2023

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Publisher Copyright:
© 2023 The Author(s).

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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, 51(17), 9369-9384. https://doi.org/10.1093/nar/gkad613

BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures. / Danino, Yehuda M.; Molitor, Lena; Rosenbaum-Cohen, Tamar; Kaiser, Sebastian; Cohen, Yahel; Porat, Ziv; Marmor-Kollet, Hagai; Katina, Corine; Savidor, Alon; Rotkopf, Ron; Ben-Isaac, Eyal; Golani, Ofra; Levin, Yishai; Monchaud, David; Hickson, Ian D.; Hornstein, Eran.

In: Nucleic Acids Research, Vol. 51, No. 17, 2023, p. 9369-9384.

Research output: Contribution to journal › Journal article › Research › peer-review

Danino, YM, 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, ID & 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. https://doi.org/10.1093/nar/gkad613

Danino, Yehuda M. ; Molitor, Lena ; Rosenbaum-Cohen, Tamar ; Kaiser, Sebastian ; Cohen, Yahel ; Porat, Ziv ; Marmor-Kollet, Hagai ; Katina, Corine ; Savidor, Alon ; Rotkopf, Ron ; Ben-Isaac, Eyal ; Golani, Ofra ; Levin, Yishai ; Monchaud, David ; Hickson, Ian D. ; Hornstein, Eran. / BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures. In: Nucleic Acids Research. 2023 ; Vol. 51, No. 17. pp. 9369-9384.

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title = "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. ",

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T1 - BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures

AU - Danino, Yehuda M.

AU - Molitor, Lena

AU - Rosenbaum-Cohen, Tamar

AU - Kaiser, Sebastian

AU - Cohen, Yahel

AU - Porat, Ziv

AU - Marmor-Kollet, Hagai

AU - Katina, Corine

AU - Savidor, Alon

AU - Rotkopf, Ron

AU - Ben-Isaac, Eyal

AU - Golani, Ofra

AU - Levin, Yishai

AU - Monchaud, David

AU - Hickson, Ian D.

AU - Hornstein, Eran

PY - 2023

Y1 - 2023

N2 - 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.

AB - 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.

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DO - 10.1093/nar/gkad613

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EP - 9384

JO - Nucleic Acids Research

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SN - 0305-1048

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