PXD018932

PXD018932 is an original dataset announced via ProteomeXchange.

Title	Whole proteome and Secretome analysis of Staphylococcus aureus ClpXP mutant strains
Description	Staphylococcus aureus represents an opportunistic pathogen which utilizes elaborate quorum sensing mechanisms to precisely control the expression and secretion of virulence factors. Previous studies indicated a role of the ClpXP proteolytic system in controlling pathogenesis. While detailed transcriptome data for ClpP and ClpX is available, corresponding studies on the proteome, secretome and metabolome level are largely lacking. In order to decipher the functional roles of ClpP and ClpX more globally we utilized S. aureus deletion mutants of the corresponding genes for in-depth proteomic LC-MS/MS analysis. These studies were complemented by a ClpP active site mutant strain to monitor changes solely depending on the presence and not the activity of the protein. A comparison of these strains with wild type revealed e.g. downregulation of virulence, purine/pyrimidine biosynthesis, iron uptake and stress response. Correspondingly, a reduction of a subset of purine and pyrimidine metabolite levels independently confirmed these results. Interestingly, comparison between the ClpP knockout and ClpP active site mutant strains revealed characteristic differences in UMP biosynthesis and the staphyloferrin B pathway, suggesting that the presence of the protein, although inactive, is important for maintaining these processes. These results are not only of fundamental importance to understand the cellular role of ClpXP but also have implications for the development of novel virulence inhibitor classes.
HostingRepository	PRIDE
AnnounceDate	2021-03-15
AnnouncementXML	Submission_2021-03-14_22:47:36.553.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Volker Kirsch
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2020-04-30 05:29:31	ID requested
1	2021-03-12 09:15:02	announced
⏵ 2	2021-03-14 22:47:37	announced	2021-03-15: Updated project metadata.

10.1021/ACS.JPROTEOME.0C00668;

Kirsch VC, Fetzer C, Sieber SA, . J Proteome Res, 20(1):867-879(2021) [pubmed]

submitter keyword: Whole proteome analysis, LC-MS/MS, proteomics, Staphylococcus aureus

Stephan A. Sieber
contact affiliation	Stephan A. Sieber, Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, Garching b. München 85747, Germany; Chair of Organic Chemistry II, Technische Universität München, Garching b. München 85747, Germany
contact email	stephan.sieber@tum.de
lab head
Volker Kirsch
contact affiliation	Technical University of Munich
contact email	volker.kirsch@tum.de
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/2021/03/PXD018932

PRIDE project URI

• PRIDE
  1. PXD018932
     1. Label: PRIDE project
     2. Name: Whole proteome and Secretome analysis of Staphylococcus aureus ClpXP mutant strains