PXD064592

PXD064592 is an original dataset announced via ProteomeXchange.

Title	Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs
Description	Phase separation (PS) of biomolecular condensates is often assumed to be driven by interactions 2 involving nucleic acids and intrinsically disordered regions (IDRs) of proteins. PGL-3 is a 3 component of P granules, biomolecular condensates in C. elegans, that contains two structured 4 domains (D1-D2), an internal IDR, and a C-terminal IDR rich with RGG motifs. Theoretical and in 5 vitro studies implicated the internal IDR and RGG motifs in driving PGL-3 PS via self-interactions 6 and binding to RNA. Studies in cells, however, implicated the D1 and D2 domains. Here, we 7 investigate the molecular basis of PGL-3 PS in vitro using microscopy, crosslinking mass 8 spectrometry and biophysical measurements. We find that D1-D2 forms oligomers and is 9 necessary and sufficient for PS. The terminal RGG region interacts with D1-D2 in a manner that 10 enhances PS even in the absence of RNA. In contrast, the internal IDR is neither necessary nor 11 sufficient for PS. These findings support an alternative model for PGL-3 PS that does not require RNA and is driven by oligomerization of structured domains that interact with RGG repeats.
HostingRepository	PRIDE
AnnounceDate	2026-03-13
AnnouncementXML	Submission_2026-03-13_09:30:17.925.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD064592
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Piyoosh Sharma
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: NEWT:562;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2025-06-03 22:11:09	ID requested
⏵ 1	2026-03-13 09:30:18	announced

10.1038/S44319-026-00730-7;

10.6019/PXD064592;

submitter keyword: None

Stephen D.
contact affiliation	Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA; Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA
contact email	sdfried@jhu.edu
lab head
Piyoosh Sharma
contact affiliation	Department of Chemistry, Johns Hopkins University, Baltimore
contact email	rx.piyush@gmail.com
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/2026/03/PXD064592

PRIDE project URI

• PRIDE
  1. PXD064592
     1. Label: PRIDE project
     2. Name: Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs