Proteomics

Dataset Information

0

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. 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 RNA-binding proteins and RNAs. BLM is enriched in SGs upon different stress conditions and in an rG4-dependent manner. We show that BLM unwinds rG4s efficiently, thus acting as a negative regulator of SG formation, potentially via its unwinding function. Altogether, our data expand the cellular activity of BLM and shed light on the function that helicases play in the dynamics of biomolecular condensates.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Alon Savidor  

LAB HEAD: Prof. Eran Hornstein

PROVIDER: PXD039534 | Pride | 2023-10-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
QEP2_13804_EHO_G37_15_1_020521.raw Raw
QEP2_13804_EHO_G37_16_1_040521.raw Raw
QEP2_13804_EHO_G37_17_1_040521.raw Raw
QEP2_13804_EHO_G37_18_1_040521.raw Raw
QEP2_13804_EHO_G37_19_1_020521.raw Raw
Items per page:
1 - 5 of 30
altmetric image

Publications


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-d  ...[more]

Similar Datasets

2020-04-30 | PXD015491 | Pride
2023-07-18 | GSE234238 | GEO
2024-05-17 | GSE219079 | GEO
2024-05-17 | GSE219082 | GEO
2024-05-17 | GSE219081 | GEO
2024-05-17 | GSE219080 | GEO
2020-11-11 | PXD015609 | Pride
2022-07-06 | PXD031877 | Pride
2018-04-30 | GSE106476 | GEO
2019-11-07 | PXD013501 | Pride