PXD062219

PXD062219 is an original dataset announced via ProteomeXchange.

Title	Quantitative mapping of methionine sensitivity to oxidation in the two-copper chaperone PcuC from Cereibacter sphaeroides
Description	Copper is typically coordinated by histidine, cysteine, or methionine residues in enzyme or chaperones and these residues are particularly sensitive to oxidation. However, it remains unclear whether copper-coordinating residues exhibit different sensitivity to oxidation compared to their non-coordinating counterparts, nor whether their oxidation susceptibility varies between the apo and copper-bound states of the protein. To evaluate this, we combined redox proteomics to structural analysis using the Cereibacter sphaeroides copper chaperone PcuC, which participates in the assembly of bacterial respiratory cytochrome oxidase. PcuC contains a canonical copper binding site made of two Met and two His (H51xnM63x22H86xM88), binding a Cu(I), and an unfolded C-terminal extension, rich in Met and His, proposed to coordinate an extra Cu atom. Our results showed that, in the apo-PcuC, Met135 in the C-terminal extension is highly sensitive to oxidation contrary to copper-coordinating Met, but that in the holo-PcuC, the presence of Cu strongly increased their sensitivity.
HostingRepository	PRIDE
AnnounceDate	2026-02-09
AnnouncementXML	Submission_2026-02-08_16:22:05.518.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Maya BELGHAZI
SpeciesList	scientific name: Cereibacter sphaeroides; NCBI TaxID: NEWT:1063; scientific name: Bacteria; NCBI TaxID: NCBITaxon:2;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2025-03-25 09:35:26	ID requested
⏵ 1	2026-02-08 16:22:06	announced

Tarrago L, Molinelli L, Belghazi M, Tribout M, Lemaire D, Legrand P, Grosse S, Pignol D, Sabaty M, Tron T, Arnoux P, Quantitative mapping of methionine sensitivity to oxidation in the copper-bound PcuC chaperone. Redox Biol, 90():104037(2026) [pubmed]

10.1016/j.redox.2026.104037;

submitter keyword: methionine oxidation, cofactor biosynthesis, periplasm,copper chaperone, oxaziridine

Lionel Tarrago
contact affiliation	Fungal Biodiversity and Biotechnology Laboratory team "Responses and adaptation of fungi to environmental constraints" 163 Avenue de Luminy, CP925 13288 Marseille, Cedex 9, FRANCE
contact email	lionel.tarrago@inrae.fr
lab head
Maya BELGHAZI
contact affiliation	CNRS
contact email	maya.belghazi@univ-amu.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD062219
     1. Label: PRIDE project
     2. Name: Quantitative mapping of methionine sensitivity to oxidation in the two-copper chaperone PcuC from Cereibacter sphaeroides