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

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

Standard

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

Harvard

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

APA

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

Vancouver

Danino YM, Molitor L, Rosenbaum-Cohen T, Kaiser S, Cohen Y, Porat Z et al. BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures. Nucleic Acids Research. 2023;51(17):9369-9384. https://doi.org/10.1093/nar/gkad613

Author

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.

Bibtex

@article{374ecfdab46349f688892ae99e0e56d4,
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. ",
author = "Danino, {Yehuda M.} and Lena Molitor and Tamar Rosenbaum-Cohen and Sebastian Kaiser and Yahel Cohen and Ziv Porat and Hagai Marmor-Kollet and Corine Katina and Alon Savidor and Ron Rotkopf and Eyal Ben-Isaac and Ofra Golani and Yishai Levin and David Monchaud and Hickson, {Ian D.} and Eran Hornstein",
note = "Publisher Copyright: {\textcopyright} 2023 The Author(s).",
year = "2023",
doi = "10.1093/nar/gkad613",
language = "English",
volume = "51",
pages = "9369--9384",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "17",

}

RIS

TY - JOUR

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

N1 - Publisher Copyright: © 2023 The Author(s).

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.

U2 - 10.1093/nar/gkad613

DO - 10.1093/nar/gkad613

M3 - Journal article

C2 - 37503837

AN - SCOPUS:85172122186

VL - 51

SP - 9369

EP - 9384

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 17

ER -

ID: 371926991