The zinc repository of Cupriavidus metallidurans
Author(s) -
Martin Herzberg,
Dirk Dobritzsch,
Stefan Helm,
Sacha Baginsky,
Dietrich H. Nies
Publication year - 2014
Publication title -
metallomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.012
H-Index - 75
eISSN - 1756-591X
pISSN - 1756-5901
DOI - 10.1039/c4mt00171k
Subject(s) - zinc , proteome , zinc finger , chemistry , mutant , biochemistry , computational biology , biology , gene , organic chemistry , transcription factor
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 the zinc ions per cell, indicating that the totality of the zinc proteome provides empty binding sites for the incoming zinc ions. This zinc repository plays a central role in zinc homeostasis in C. metallidurans and probably also in other organisms.
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