PXD013495-2

PXD013495 is an original dataset announced via ProteomeXchange.

Title	Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites
Description	Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of peptide-centric chemoproteomics, 1,537 S-sulfenylated sites were mapped on more than 1,000 proteins in Arabidopsis thaliana cells. The H2O2 sensitivity was quantified of more than 70% of these endogenous oxidation events toward exogenous H2O2 stimulation. Proteins involved in RNA and metabolic processing were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located in catalytic sites of enzymes or on cysteines involved in metal binding, hinting at direct mode-of-actions for redox regulation. Comparison of human and Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which is speculated to be a redox-regulatory site. Replacement of the noncatalytic Cys181 of the recombinant AtMAPK4 by the redox-insensitive serine decreased the protein kinase activity, emphasizing the importance of this noncatalytic cysteine. Altogether, we quantitatively mapped the S-sulfenylated cysteines in Arabidopsis plants under oxidative stress and delivered an unprecedented inventory for unraveling the precise role of these oxidized cysteines in plant redox signaling.
HostingRepository	PRIDE
AnnounceDate	2019-09-16
AnnouncementXML	Submission_2019-10-07_02:38:52.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jing Yang
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2019-04-15 01:49:04	ID requested
1	2019-09-16 01:11:04	announced
⏵ 2	2019-10-07 02:38:53	announced	2019-10-07: Updated publication reference for PubMed record(s): 31578252.
3	2024-10-22 04:55:59	announced	2024-10-22: Updated project metadata.

Huang J, Willems P, Wei B, Tian C, Ferreira RB, Bodra N, Mart, í, nez Gache SA, Wahni K, Liu K, Vertommen D, Gevaert K, Carroll KS, Van Montagu M, Yang J, Van Breusegem F, Messens J, uncovers redox-sensitive sites. Proc Natl Acad Sci U S A, 116(42):21256-21261(2019) [pubmed]

submitter keyword: Chemoproteomics, BTD, Sulfenic acid

Jing Yang
contact affiliation	jState Key Laboratory of Proteomics, Beijing Proteome Research Center (BPRC), National Center for Protein Sciences, Beijing, Institute of Lifeomics, Beijing 102206, China
contact email	yangjing54@hotmail.com
lab head
Jing Yang
contact affiliation	National Center for Protein Sciences, Beijing
contact email	yangjing54@hotmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD013495
     1. Label: PRIDE project
     2. Name: Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites