PXD007167

PXD007167 is an original dataset announced via ProteomeXchange.

Title	Spectral library based analysis of arginine phosphorylations in Staphylococcus aureus
Description	Reversible protein phosphorylation is one of the major mechanisms in the regulation of protein expression and protein activity, controlling physiological functions of the important human pathogen Staphylococcus aureus. Phosphorylations at serine, threonine and tyrosine are known to influence for example protein activity in central metabolic pathways and the more energy-rich phosphorylations at histidine, aspartate or cysteine can be found as part of two component system sensor domains or mediating bacterial virulence. In addition to these well-known phosphorylations, the phosphorylation at arginine residues plays an essential role. Hence, the deletion mutant S. aureus COL ΔptpB (protein tyrosine phosphatase B) was studied since the protein PtpB is assumed to be an arginine phosphatase. A gel-free approach was applied to analyse the changes in the phosphoproteome of the deletion mutant ΔptpB and the wild type in growing cells, thereby focusing on the occurrence of phosphorylation on arginine residues. In order to enhance the reliability of identified phosphorylation sites at arginine residues, a subset of arginine phosphorylated peptides was chemically synthesised. Combined spectral libraries based on phosphoenriched samples, synthetic arginine phosphorylated peptides and classical proteome samples provide a sophisticated tool for the analysis of arginine phosphorylations. This way, 212 proteins phosphorylated on serine, threonine, tyrosine or arginine residues were identified within the mutant ∆ptpB and 102 in wild type samples. Among them, 207 arginine phosphosites were identified exclusively within the mutant ∆ptpB, widely distributed along the whole bacterial metabolism. This identification of putative targets of PtpB allows further investigation of the physiological relevance of arginine phosphorylations and provides the basis for reliable quantification of arginine phosphorylations in bacteria.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:40:03.491.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sandra Maass
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2017-08-02 02:43:20	ID requested
1	2017-12-06 05:41:24	announced
⏵ 2	2024-10-22 04:40:09	announced	2024-10-22: Updated project metadata.

Junker S, Maa, β S, Otto A, Michalik S, Morgenroth F, Gerth U, Hecker M, Becher D, . Mol Cell Proteomics, 17(2):335-348(2018) [pubmed]

10.1074/mcp.ra117.000378;

curator keyword: Biological

submitter keyword: Staphylococcus aureus, gel-free proteomics,arginine phosphorylation, phosphopeptide enrichment, spectral library

Dörte Becher
contact affiliation	Institute for Microbiology, Department of Microbial Proteomics, Ernst Moritz Arndt University Greifswald, Germany
contact email	dbecher@uni-greifswald.de
lab head
Sandra Maass
contact affiliation	University of Greifswald, Department for Microbial Proteomics
contact email	sandra.maass@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD007167
     1. Label: PRIDE project
     2. Name: Spectral library based analysis of arginine phosphorylations in Staphylococcus aureus