| Literature DB >> 25315396 |
Martin Herzberg1, Dirk Dobritzsch, Stefan Helm, Sacha Baginsky, Dietrich H Nies.
Abstract
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.Entities:
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Year: 2014 PMID: 25315396 DOI: 10.1039/c4mt00171k
Source DB: PubMed Journal: Metallomics ISSN: 1756-5901 Impact factor: 4.526