PXD009874-3

PXD009874 is an original dataset announced via ProteomeXchange.

Title	Toward the quantitative characterization of arginine phosphorylations in Staphylococcus aureus
Description	The Gram positive bacterium Staphylococcus aureus plays an important role as an opportunistic pathogen and causative agent of nosocomial infections. As research gained insight into host specific adaptation and a broad range of virulence mechanisms, S. aureus evolved as a model organism for human pathogens. Hence, the investigation of staphylococcal proteome expression and regulation supports the understanding of the pathogenicity and relevant physiology of this organism. This study focused on the analysis of protein regulation by reversible protein phosphorylation, in particular on arginine residues. Therefore, both proteome and phosphoproteome of S. aureus COL wild type were compared with the arginine phosphatase deletion mutant S. aureus COL ΔptpB under control and stress conditions in a quantitative manner. A gel-free approach, adapted to the special challenges of arginine phosphorylation, was applied to analyze the phosphoproteome of exponential growing cells after oxidative stress caused by sublethal concentrations of H2O2. Together with phenotypic characterization of S. aureus COL ΔptpB, this study disclosed first insights into the physiological role of arginine phosphorylations in Gram positive pathogens. The spectral library based quantification of phosphopeptides finally allowed to link arginine phosphorylation to staphylococcal oxidative stress response, amino acid metabolism and virulence.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:13:42.680.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sabryna Junker
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	2018-05-24 00:55:31	ID requested
1	2018-10-29 09:32:46	announced
2	2018-10-31 05:30:53	announced	Updated publication reference for PubMed record(s): 30358407.
⏵ 3	2024-10-22 04:13:47	announced	2024-10-22: Updated project metadata.

10.1021/acs.jproteome.8b00579;

Junker S, Maa, ß S, Otto A, Hecker M, Becher D, Toward the Quantitative Characterization of Arginine Phosphorylations in Staphylococcus aureus. J Proteome Res, 18(1):265-279(2019) [pubmed]

curator keyword: Biomedical

submitter keyword: virulence, SILAC quantification, Staphylococcus aureus, amino acid metabolism,arginine phosphorylation, oxidative stress, phosphopeptide enrichment, hydrogen peroxide, spectral library, quantification

Dörte Becher
contact affiliation	Institute for Microbiology, Department of Microbial Proteomics, University of Greifswald, Greifswald, Germany
contact email	dbecher@uni-greifswald.de
lab head
Sabryna Junker
contact affiliation	Institute for Microbiology
contact email	sabryna.junker@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009874
     1. Label: PRIDE project
     2. Name: Toward the quantitative characterization of arginine phosphorylations in Staphylococcus aureus