PXD020226

PXD020226 is an original dataset announced via ProteomeXchange.

Title	In depth characterization of the S. aureus phosphoproteome reveals new targets of Stk1
Description	Staphylococcus aureus is the leading cause of infections worldwide and infection results in a variety of diseases. As of no surprise, phosphorylation is a major game player in signaling cascades and has been shown to be involved in S. aureus virulence. Albeit long neglected, eukaryotic-like serine/threonine kinases have been implicated in these complex signaling cascades. Due to the sub-stoichiometric nature of protein phosphorylation and a lack of suitable analysis tools, the knowledge of these cascades is however, to date, still limited. Here, were apply an optimized protocol for efficient phosphopeptide enrichment via Fe3+-IMAC followed by LC-MS/MS to get a better understanding of the impact of protein phosphorylation on the complex signaling networks involved in pathogenicity. By profiling a serine/threonine kinase and phosphatase mutant from a methicillin-resistant S. aureus mutant library, we generated the most comprehensive phosphoproteome dataset of S. aureus to date, aiding a better understanding of signaling in bacteria.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:17:00.157.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nadine Prust
SpeciesList	scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308; scientific name: Staphylococcus aureus (strain USA300); NCBI TaxID: 367830;
ModificationList	phosphorylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-07-06 15:12:25	ID requested
1	2020-12-21 03:55:31	announced
⏵ 2	2024-10-22 05:17:00	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: phosphoproteome, Staphylococcus aureus,Bacteria, Stk1

Simone Lemeer
contact affiliation	Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands
contact email	S.M.Lemeer@uu.nl
lab head
Nadine Prust
contact affiliation	Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands
contact email	n.prust@uu.nl
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/PXD020226

PRIDE project URI

• PRIDE
  1. PXD020226
     1. Label: PRIDE project
     2. Name: In depth characterization of the S. aureus phosphoproteome reveals new targets of Stk1