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The zinc repository of Cupriavidus metallidurans

ABSTRACT: Zinc is a central player in the metalloproteomes of prokaryotes and eukaryotes. We used a top-down quantitative proteomic approach to reveal the repository of the zinc pools in the proteobacterium Cupriavidus metallidurans. About 60% of the theoretical proteome of C. metallidurans were identified, quantified, and compared between a ΔzupT mutant defect in zinc allocation and its parent strain. In both strains, the number of zinc-binding proteins and their binding sites exceeded that of the zinc ions per cell, indicating that the totality of the zinc proteome provides empty binding sites for incoming zinc ions. This zinc repository plays a central role in zinc homeostasis in C. metallidurans and probably also in other organisms.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Cupriavidus Metallidurans

TISSUE(S): Prokaryotic Cell

SUBMITTER: Sacha Baginsky

LAB HEAD: Baginsky, Sacha

PROVIDER: PXD001356 | Pride | 2016-05-04

REPOSITORIES: Pride

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			Action	DRS
	MH1_120917_001.raw.zip	Raw
	MH1_120917_001.zip	Other
	MH1_120917_003.raw.zip	Raw
	MH1_120917_003.zip	Other
	MH1_120917_004.raw.zip	Raw

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The zinc repository of Cupriavidus metallidurans.

Herzberg Martin M Dobritzsch Dirk D Helm Stefan S Baginsky Sacha S Nies Dietrich H DH

Metallomics : integrated biometal science 20141101 11

Zinc is a central player in the metalloproteomes of prokaryotes and eukaryotes. We used a bottom-up quantitative proteomic approach to reveal the repository of the zinc pools in the proteobacterium Cupriavidus metallidurans. About 60% of the theoretical proteome of C. metallidurans was identified, quantified, and the defect in zinc allocation was compared between a ΔzupT mutant and its parent strain. In both strains, the number of zinc-binding proteins and their binding sites exceeded that of th ...[more]

PMID: 25315396

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