PXD014928

PXD014928 is an original dataset announced via ProteomeXchange.

Title	Proteome-wide identification of in vitro substrates for P. aeruginosa ClpXP
Description	we treated the cell lysates of ΔclpX mutant with or without P. aeruginosa ClpXP protease and used Label-free quantitative techniques (LFQ) to identify and quantify the proteolytic targets of ClpXP (p.aeruginosa PAO1). As a result, 3338 proteins were identified and 2493 proteins were quantified. The abundance (LFQ intensity) of 44 proteins were decreased (≥1.5-fold, p < 0.05) by the treatment with ClpXP. Moreover, we observed that there are 31 proteins which have valid LFQ intensity values in all the three biological replicates of the control group but not in the experimental group (i.e., ClpXP-treated). These results suggest that exogenously added ClpXP has a profound effect on the abundance of proteins in our in vitro assays and that those 75 proteins may serve as potential substrates for the P. aeruginosa ClpXP.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:02:49.574.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nana Yang
SpeciesList	scientific name: Pseudomonas aeruginosa PAO1; NCBI TaxID: 208964;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-08-06 05:27:29	ID requested
1	2020-04-29 02:42:07	announced
⏵ 2	2024-10-22 05:02:53	announced	2024-10-22: Updated project metadata.

Yang N, Cao Q, Hu S, Xu C, Fan K, Chen F, Yang CG, Liang H, Wu M, Bae T, Lan L, Alteration of protein homeostasis mediates the interaction of Pseudomonas aeruginosa with Staphylococcus aureus. Mol Microbiol, 114(3):423-442(2020) [pubmed]

10.1111/mmi.14519;

submitter keyword: proteolytic targets, Label-free Quantification LC-MS/MS, p.aeruginosa PAO1,ClpXP

Lefu Lan
contact affiliation	Shanghai Institute of Materia Medica, Chinese Academy of Sciences
contact email	llan@simm.ac.cn
lab head
Nana Yang
contact affiliation	Shanghai Institute of Materia Medica, Chinese Academy of Sciences
contact email	yaodou888@126.com
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/2020/04/PXD014928

PRIDE project URI

• PRIDE
  1. PXD014928
     1. Label: PRIDE project
     2. Name: Proteome-wide identification of in vitro substrates for P. aeruginosa ClpXP