PXD019928

PXD019928 is an original dataset announced via ProteomeXchange.

Title	Profiling thimet oligopeptidase-mediated proteolysis in Arabidopsis thaliana
Description	Plant stress caused by pathogens or though abiotic means (e.g. drought or temperature) reduces agricultural yields, causing substantial economic losses while reducing food security at the global level. It is critical to recognize how plants perceive stress signals to elicit responses for survival. Endogenous plant peptidases and their peptide products play an important role in the signaling of plant immune processes. Thimet oligopeptidases (TOPs) are zinc-dependent peptide hydrolases with a conserved HEXXH active site motif. These metallopeptidases are critical components in plant response to oxidative stress triggered by pathogens or abiotic factors and are required for a fully functioning immune response to certain pathogens. Further characterization of plant TOPs and their peptide substrates would provide insights into their contribution to defense signaling, stress perception, and plant adaptation pathways. Herein, a quantitative mass spectrometry-based peptidomics approach was implemented to characterize the Arabidopsis thaliana plant peptidome and in the context TOPs (Fig. 1). A comparison between wild type (Col-0) and top1top2 null mutant revealed putative direct and indirect TOPs substrates in vivo.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:18:04.635.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD019928
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Leslie Hicks
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	amidated residue; monohydroxylated residue; acetylated residue
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-22 03:08:18	ID requested
1	2021-03-04 13:01:06	announced
⏵ 2	2024-10-22 05:18:06	announced	2024-10-22: Updated project metadata.

10.1111/tpj.15165;

Iannetta AA, Rogers HT, Al-Mohanna T, O'Brien JN, Wommack AJ, Popescu SC, Hicks LM, Profiling thimet oligopeptidase-mediated proteolysis in Arabidopsis thaliana. Plant J, 106(2):336-350(2021) [pubmed]

10.6019/PXD019928;

submitter keyword: TOPs,Arabidopsis, thimet oligopeptidases, peptidome

Leslie Hicks
contact affiliation	Department of Chemistry, The University of North Carolina at Chapel Hill, Chapel Hill, NC
contact email	lmhicks@live.unc.edu
lab head
Leslie Hicks
contact affiliation	University of North Carolina at Chapel Hill
contact email	lmhicks@unc.edu
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/2021/01/PXD019928

PRIDE project URI

• PRIDE
  1. PXD019928
     1. Label: PRIDE project
     2. Name: Profiling thimet oligopeptidase-mediated proteolysis in Arabidopsis thaliana