PXD024059

PXD024059 is an original dataset announced via ProteomeXchange.

Title	The plant thimet oligopeptidases TOP1 and TOP2 have divergent redox sensitivities and substrate cleavage specificity
Description	Physiological and pathogen-induced oscillations in the plant cells' redox environment trigger response mechanisms that involve redox-sensitive cysteines and consequent changes in proteins' biochemical and functional characteristics. Arabidopsis thimet oligopeptidases (TOPs) TOP1 and TOP2 are components of the immune signaling and oxidative stress response. Here, TOP1 and TOP2 were evaluated comparatively to understand their role as redox sensors. We show that TOPs catalytic activity is augmented in plants undergoing an immune response and in mutant lines with altered expression of the chloroplastic NTRC impaired in the chloroplast thiol-disulfide regulatory system; ntrc was unable to mount a systemic immune response. Oxidation promoted TOP1 self-interaction to dimers and oligomers; Cys-to-Ala mutagenesis of multiple Cys residues inhibited TOP1 oxidative self-interaction. In contrast, TOP1 lacking the signal peptide (ΔSPTOP1) and TOP2 were detected solely as monomers. Treatment with oxidized glutathione increased the catalytic activities of TOPs; Ala substitution of the unique Cys405 of TOP2 abolished its oxidative activation. The immune regulator ROC1 was identified as a candidate TOPs substrate. TOPs cleaved a ROC1 peptide (ROC1p) at similar and unique cleavage sites; ROC1p concentration helped determine TOPs cleavage specificity. We propose that TOP1 and TOP2 form a proteolysis couple with divergent redox-sensing mechanisms and specificity.
HostingRepository	PRIDE
AnnounceDate	2021-04-19
AnnouncementXML	Submission_2021-04-19_08:28:31.354.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD024059
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Leslie Hicks
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	acetylated residue; monohydroxylated residue
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2021-02-08 07:17:58	ID requested
⏵ 1	2021-04-19 08:28:31	announced

Dataset with its publication pending

submitter keyword: thimet oligopeptidase, Arabidopsis, redox regulation

Leslie Hicks
contact affiliation	Associate Professor, Chemistry Department, University of North Carolina at Chapel Hill
contact email	lmhicks@unc.edu
lab head
Leslie Hicks
contact affiliation	University of North Carolina at Chapel Hill
contact email	lmhicks@unc.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD024059
     1. Label: PRIDE project
     2. Name: The plant thimet oligopeptidases TOP1 and TOP2 have divergent redox sensitivities and substrate cleavage specificity