PXD029475

PXD029475 is an original dataset announced via ProteomeXchange.

Title	Clostridioides difficile phosphoproteomics shows an expansion of phosphorylated proteins in stationary growth phase
Description	Phosphorylation is a post-translational modification that can affect both house-keeping functions and virulence characteristics in bacterial pathogens. In the Gram-positive enteropathogen Clostridioides difficile the extent and nature of phosphorylation events is poorly characterized, though a protein-kinase mutant strain demonstrates pleiotropic phenotypes. Here, we used an immobilized metal affinity chromatography strategy to characterize serine, threonine and tyrosine phosphorylation in C. difficile. We find limited protein phosphorylation in the exponential growth phase but a sharp increase in the number of phosphopeptides after the onset of stationary growth phase. Among the overall more than 1500 phosphosites, our approach identifies expected targets and phosphorylation sites, including the protein kinase PrkC, the anti-sigma-F factor antagonist (SpoIIAA), the anti-sigma-B factor antagonist (RsbV) and HPr kinase/phosphorylase (HprK).. Analysis of high-confidence phosphosites shows that phosphorylation on serine residues is most common, followed by threonine and tyrosine phosphorylation. This work forms the basis for a further investigation into the contributions of individual kinases to the overall phosphoproteome of C. difficile and the role of phosphorylation in C. difficile physiology and pathogenesis.
HostingRepository	PRIDE
AnnounceDate	2022-02-16
AnnouncementXML	Submission_2022-02-16_15:19:02.717.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Yassene Mohammed
SpeciesList	scientific name: Clostridioides difficile 630; NCBI TaxID: 272563;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-01 05:01:23	ID requested
⏵ 1	2022-02-16 15:19:03	announced

Smits WK, Mohammed Y, de Ru AH, Cordo' V, Friggen AH, van Veelen PA, Hensbergen PJ, Clostridioides difficile Phosphoproteomics Shows an Expansion of Phosphorylated Proteins in Stationary Growth Phase. mSphere, 7(1):e0091121(2022) [pubmed]

submitter keyword: Clostridioides difficile, phosphoproteomics

Paul J. Hensbergen
contact affiliation	Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
contact email	P.J.Hensbergen@lumc.nl
lab head
Yassene Mohammed
contact affiliation	LUMC/UVIC
contact email	y.mohammed@lumc.nl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD029475
     1. Label: PRIDE project
     2. Name: Clostridioides difficile phosphoproteomics shows an expansion of phosphorylated proteins in stationary growth phase