PXD022403 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Discovery of arginine methylation, phosphorylation and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae |
Description | The formation of condensates in membraneless organelles is thought to be driven by protein phase separation. Arginine methylation and serine/threonine phosphorylation are important in the phase separation process, however these post-translational modifications are often present in intrinsically disordered regions that are difficult to analyse with standard proteomic techniques. Here we use a multi-protease and multi-MS/MS fragmentation approach, coupled with heavy methyl SILAC and phospho- or methyl-peptide enrichment, for the analysis of arginine methylation and serine/threonine phosphorylation, and to understand their co-occurrence in condensate-associated proteins. For Saccharomyces cerevisiae, we report a 50% increase in the known arginine methylproteome, involving 15 proteins that are almost all condensate-associated. Importantly, some of these proteins have arginine methylation on all predicted sites – providing evidence that this modification can be pervasive. We explored whether arginine methylated condensate-associated proteins are also phosphorylated, and found 12 such proteins to carry phosphoserine or phosphothreonine. In Npl3, Ded1 and Ssbp1, single peptides were found to carry both modifications, indicating a co-occurrence in close proximity and on the same protein molecule. We show that these co-modifications occur in regions of disorder and that arginine methylation is typically on basic regions of disorder. For phosphorylation, its association with charged regions of condensate-associated proteins was less consistent, although some regions with multisite phosphorylation sites were strongly acidic. We conclude that arginine-methylated proteins associated with condensates are typically co-modified with protein phosphorylation. |
HostingRepository | PRIDE |
AnnounceDate | 2021-09-21 |
AnnouncementXML | Submission_2021-09-21_02:57:25.787.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Joshua Hamey |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | monomethylated residue; phosphorylated residue; methylated arginine; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion Lumos; Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-11-06 01:39:30 | ID requested | |
1 | 2021-09-16 21:47:05 | announced | |
⏵ 2 | 2021-09-21 02:57:26 | announced | 2021-09-21: Updated project metadata. |
Publication List
Keyword List
submitter keyword: yeast,methylation, phosphorylation, crosstalk |
Contact List
Marc Wilkins |
contact affiliation | School of Biotechnology and Biomolecular Sciences, University of New South Wales, NSW, Australia |
contact email | m.wilkins@unsw.edu.au |
lab head | |
Joshua Hamey |
contact affiliation | University of New South Wales |
contact email | j.hamey@unsw.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD022403
- Label: PRIDE project
- Name: Discovery of arginine methylation, phosphorylation and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae