Dataset Information

Quantitative mapping of methionine sensitivity to oxidation in the two-copper chaperone PcuC from Cereibacter sphaeroides

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Cereibacter Sphaeroides Bacteria

SUBMITTER: Maya BELGHAZI

LAB HEAD: Lionel Tarrago

PROVIDER: PXD062219 | Pride | 2026-02-09

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	2022-0102-R1-TMT-PCuAcH2O2.mgf	Mgf
	2022-0102-R1-TMT-PCuAcH2O2.raw	Raw
	2022-0302-R2-TMT-PcuAcH2O2.mgf	Mgf
	2022-0302-R2-TMT-PcuAcH2O2.raw	Raw
	2022-0302-R2-TMT-PcuAcOXA.mgf	Mgf

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Publications

Quantitative mapping of methionine sensitivity to oxidation in the copper-bound PcuC chaperone.

Tarrago Lionel L Molinelli Lise L Belghazi Maya M Tribout Mathilde M Lemaire David D Legrand Pierre P Grosse Sandrine S Pignol David D Sabaty Monique M Tron Thierry T Arnoux Pascal P

Redox biology 20260119

Copper is typically coordinated by histidine, cysteine, or methionine in proteins, and these residues are particularly sensitive to oxidation. However, it remains unclear whether copper-coordinating residues are more prone to oxidation than non-coordinating ones, and how their susceptibility changes between the apo and copper-bound states. The copper chaperone PcuC, important for cytochrome c oxidase assembly in bacteria, contains a canonical binding site composed of two histidines and two methi ...[more]

PMID: 41579735

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Project description:Copper and iron are essential micronutrients for most living organisms because they participate as cofactors in biological processes including respiration, photosynthesis and oxidative stress protection. In many eukaryotic organisms, including yeast and mammals, copper and iron homeostases are highly interconnected; however such interdependence is not well established in higher plants. Here we propose that COPT2, a high-affinity copper transport protein, functions under copper and iron deficiencies in Arabidopsis thaliana. COPT2 is a plasma membrane protein that functions in copper acquisition and distribution. Characterization of the COPT2 expression pattern indicates a synergic response to copper and iron limitation in roots. We have characterized a knockout of COPT2, copt2-1, that leads to increased resistance to simultaneous copper and iron deficiencies, measured as reduced leaf chlorosis and improved maintenance of the photosynthetic apparatus. We propose that COPT2 expression could play a dual role under Fe deficiency. First, COPT2 participates in the attenuation of copper deficiency responses driven by iron limitation maybe aimed to minimize further iron consume. On the other hand, global expression analyses of copt2-1 mutants versus wild type Arabidopsis plants indicate that low phosphate responses are increased in copt2-1 plants. In this sense, COPT2 function under Fe deficiency counteracts low phosphate responses. These results open up new biotechnological approaches to fight iron deficiency in crops. Four biological replicates of Arabidopsis seedlings were generated for 2 genotypes, Col-0 and copt2-1 mutant; and 3 growth condictions; first one an iron(Fe) and copper(Cu) sufficient medium (+Fe + Cu), second one an Fe deficient and Cu sufficient medium (-Fe+Cu) and third one an Fe and Cu deficient medium (-Fe-Cu). For each growth one comparasion was made, copt2-1 mutant versus Col-0; in each comparasion four biological replicates were made, two replicas were labeled with Cy5 for the mutant sample and Cy3 for the Col-0 sample, while the other two replicas were reversed-labeled.