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PXD043477-1

PXD043477 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleIdentification of active papain-like cysteine proteases in the flag leaf of naturally senescing and ozone-exposed wheat plants.
DescriptionCurrent tropospheric ozone (O3) background concentrations have significant adverse effects on wheat. O3 generally induces oxidative damages and premature leaf senescence leading to important yield losses. As vacuolar Endoproteases (EP) are involved in both maintaining cell longevity during abiotic stresses and performing efficient nitrogen remobilization during leaf senescence, we aimed to characterize acidic endoproteolytic activities involved during natural and O3-induced flag leaf senescence in wheat. Two winter wheat cultivars (cvs.) with different O3 sensitivity, Soissons and Premio, were grown in the field at the experimental farm of AgroParisTech (Thiverval Grignon, France) and exposed to ambient (AOT40 = 1.58 ppm.h) and semi-controlled chronic O3 concentrations (AOT40 = 3.71 ppm.h), from pre-anthesis to grain harvest. Flag leaf total EP activity and the major catalytic classes involved were determined using azocasein and class-specific inhibitors, respectively. Activity-based protein profiling (ABPP) was used to identify the major active cysteine proteases involved in natural and O3-induced leaf senescence. Our analysis revealed that natural leaf senescence and O3 stress induced a stimulation of endoproteolytic activities. In both cases, global leaf endoproteolytic activity was mostly due to papain-like cysteine proteases (PLCPs). ABPP analyses using DCG-04 revealed an increase in active PLCP contents in wheat flag leaf in response to O3 for both cvs. A pull-down of active PLCPs in the naturally senescing and O3-exposed flag leaf of cv. Premio was carried out and active PLCPs were identified using LC-MS/MS. Mass spectrometry analyses revealed that triticain was the major active PLCP in senescing flag leaf and also the only PLCP whom abundance was increased by O3 stress. Gene expression analysis by qPCR indicated that triticain activity could be regulated at the transcriptional level.
HostingRepositoryPRIDE
AnnounceDate2026-09-01
AnnouncementXMLSubmission_2026-09-01_09:03:20.837.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterThierry Balliau
SpeciesList scientific name: Triticum aestivum (Wheat); NCBI TaxID: NEWT:4565;
ModificationList(R)-5-oxo-1; 2-pyrrolidone-5-carboxylic acid (Glu); 2-pyrrolidone-5-carboxylic acid (Gln); acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentLTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-07-03 03:11:07ID requested
12026-09-01 09:03:21announced
Publication List
10.1016/j.plaphy.2024.109380;
Hav, é M, Espinasse C, Cottyn-Boitte B, Puga-Freitas R, Bagard M, Balliau T, Zivy M, Ganeshan S, Chibbar RN, Castell JF, Bethenod O, Leitao L, Repellin A, Triticain alpha represents the major active papain-like cysteine protease in naturally senescing and ozone-treated leaves of wheat. Plant Physiol Biochem, 219():109380(2025) [pubmed]
Keyword List
submitter keyword: Activity-Based Protein Profiling,Tropospheric ozone, Wheat (Triticum aestivum L.), Flag leaf senescence, Triticain alpha, Papain-Like Cysteine Protease
Contact List
Marien HAVE
contact affiliationInstitute of Ecology and Environmental Sciences of Paris (iEES Paris), Univ Paris Est Creteil, CNRS, INRAE, IRD, IEES, F-94010, Creteil, France
contact emailmarien.have@u-pec.fr
lab head
Thierry Balliau
contact affiliationPlateforme d'Analyse Proteomique Paris Sud-Ouest Université Paris-Saclay, INRAE, CNRS, AgroParisTech, GQE - Le Moulon, 91190, Gif-sur-Yvette, France
contact emailthierry.balliau@inrae.fr
dataset submitter
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