PXD061767

PXD061767 is an original dataset announced via ProteomeXchange.

Title	New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
Description	Persulfidation, a posttranslational modification of cysteines to persulfides, is the best characterized molecular mechanism of H2S signaling. This study is focused on new functions for thioredoxins (TRXs) in plants beyond those of thiol disulfide (S-S) exchange, including the regulation of protein persulfidation as it has been described in animal systems. To elucidate the impact of TRXo1 deficiency on the protein persulfidation pattern in plants of Arabidopsis thaliana L. wild-type (WT) and two Attrxo1 T-DNA insertion mutants grown under non stress conditions, a quantitative proteomic approach was performed. The proteomic analysis revealed a higher number of proteins that were more persulfidated in the mutants compared to WT plants, suggesting a role for TRXo1 in protein depersulfidation. Interestingly, most of the differentially persulfidated proteins were located in the chloroplast, implying a coordination between chloroplast H2S-dependent persulfidation and mitochondrial TRXo1 depersulfidation. Among the differentially persulfidated proteins located in mitochondria, the antioxidant enzymes sAPX, DHAR1, and MDAR6 were selected for further studies. The effect of H2S-dependent persulfidation on their enzymatic activities and its reversibility by the NADPH/thioredoxin reductase (NTRB)/TRXo1 system was analyzed, as well as their persulfidation levels were quantified. Sulfide treatment brought about increases in the activity levels of the enzymes, that match with a raise on the persulfidation levels. Interestingly, both activations declining after treatment with the thioredoxin system, indicating regulation of their persulfidation by TRXo1. These results point to a positive effect of persulfidation on the enzymatic activities and also to a new depersulfidase activity for TRXo1. All together these results give a new insight of the mechanism of elimination of -SSH groups in plants exerted by TRXo1, and the involvement of a redox regulation on the protein persulfidation.
HostingRepository	PRIDE
AnnounceDate	2025-05-07
AnnouncementXML	Submission_2025-05-07_07:55:25.846.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ibon Iloro
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	No PTMs are included in the dataset
Instrument	Bruker Daltonics timsTOF series

Revision	Datetime	Status	ChangeLog Entry
0	2025-03-12 10:56:46	ID requested
⏵ 1	2025-05-07 07:55:26	announced

10.1016/j.redox.2025.103627;

De Brasi-Velasco S, Aroca A, Romero LC, Gotor C, Sevilla F, Jim, é, nez A, New role for thioredoxins in plants: Implication of TRXo1 in protein depersulfidation. Redox Biol, 82():103627(2025) [pubmed]

submitter keyword: monodehydroascorbate reductase,ascorbate peroxidase, persulfidation, thioredoxin o1, hydrogen sulfide, dehydroascorbate reductase, redox regulation

Ana Jiménez
contact affiliation	Centro de Edafología y Biología Aplicada del Segura-CSIC, Murcia, Spain
contact email	ajimenez@cebas.csic.es
lab head
Ibon Iloro
contact affiliation	CIC bioGUNE
contact email	iiloro@cicbiogune.es
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD061767
     1. Label: PRIDE project
     2. Name: New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation