PXD021214-1

PXD021214 is an original dataset announced via ProteomeXchange.

Title	Post-translational modification profiling of Saccharomyces cerevisiae histone methylation enzymes uncovers regulation by upstream signalling pathways
Description	Histone methylation is central to the regulation of eukaryotic transcription. In Saccharomyces cerevisiae, it is controlled by a system of four methyltransferases (Set1p, Set2p, Set5p, and Dot1p) and four demethylases (Jhd1p, Jhd2p, Rph1p, and Gis1p). While the histone targets for these enzymes are well characterised, the connection of the enzymes with the intracellular signalling network and thus their regulation is poorly understood, in yeast and in all other eukaryotes. Here we report the detailed characterisation of the eight S. cerevisiae enzymes, and show that they carry a total of 75 phosphorylation sites, 93 acetylation sites, and two ubiquitination sites. All enzymes are subject to phosphorylation, although demethylases Jhd1p and Jhd2p contained one and five sites respectively whereas other enzymes carried 14 to 36 sites. Phosphorylation was absent or under-represented on catalytic and other domains but strongly enriched for regions of disorder on methyltransferases, suggesting a role in the modulation of protein-protein interactions. We show that a phosphorylation cluster within an acidic and intrinsically disordered N-terminal region of methyltransferase Set2p regulates H3K36 methylation levels in vivo, thus supporting the functional relevance of disordered phosphosites. While most kinases upstream of the yeast histone methylation enzymes remain unknown, we model the possible connections between the signalling network and the histone-based gene regulatory system and propose an integrated regulatory structure. Our results provide a foundation for future, detailed exploration of the role of specific kinases and phosphosites in the regulation of histone methylation.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:35:28.123.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ryan Separovich
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	monomethylated residue; adenosine diphosphoribosyl (ADP-ribosyl) modified residue; ubiquitinylated lysine; dimethylated L-arginine; phosphorylated residue; sumoylated lysine; N6-crotonyl-L-lysine; acetylated residue; monohydroxylated residue; N6,N6,N6-trimethyl-L-lysine; iodoacetamide derivatized residue; N6,N6-dimethyl-L-lysine
Instrument	Orbitrap Fusion Lumos; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2020-08-31 01:48:41	ID requested
⏵ 1	2024-10-07 13:35:28	announced

Dataset with its publication pending

submitter keyword: Histone methylation,Yeast, Post-translational modification, Epigenetics, Kinase, Phosphorylation

Marc Ronald Wilkins
contact affiliation	School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia
contact email	m.wilkins@unsw.edu.au
lab head
Ryan Separovich
contact affiliation	University of New South Wales
contact email	r.separovich@unsw.edu.au
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/2020/12/PXD021214

PRIDE project URI

• PRIDE
  1. PXD021214
     1. Label: PRIDE project
     2. Name: Post-translational modification profiling of Saccharomyces cerevisiae histone methylation enzymes uncovers regulation by upstream signalling pathways