PXD039534-2

PXD039534 is an original dataset announced via ProteomeXchange.

Title	BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures
Description	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.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:08:44.683.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alon Savidor
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2023-01-18 06:52:38	ID requested
1	2023-10-24 12:04:23	announced
⏵ 2	2023-11-14 09:08:45	announced	2023-11-14: Updated project metadata.
3	2024-10-22 06:09:28	announced	2024-10-22: Updated project metadata.

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, BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures. Nucleic Acids Res, 51(17):9369-9384(2023) [pubmed]

submitter keyword: stress granule, apex, Helicase, LC-msms,G-quadruplex, rG4-binding proteins, BLM, QUMA-1

Prof. Eran Hornstein
contact affiliation	Department of Molecular Genetics Faculty of Biochemistry Weizmann Institute of Science Rehovot, Israel
contact email	eran.hornstein@weizmann.ac.il
lab head
Alon Savidor
contact affiliation	The Weizmann Institute of Science
contact email	alon.savidor@weizmann.ac.il
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/10/PXD039534

PRIDE project URI

• PRIDE
  1. PXD039534
     1. Label: PRIDE project
     2. Name: BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures