Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/94215
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Type: Journal article
Title: ZnuA and zinc homeostasis in pseudomonas aeruginosa
Author: Pederick, V.
Eijkelkamp, B.
Begg, S.
Ween, M.
McAllister, L.
Paton, J.
McDevitt, C.
Citation: Scientific Reports, 2015; 5(1):13139-1-13139-14
Publisher: Nature
Issue Date: 2015
ISSN: 2045-2322
2045-2322
Statement of
Responsibility: 
Victoria G. Pederick, Bart A. Eijkelkamp, Stephanie L. Begg, Miranda P. Ween, Lauren J. McAllister, James C. Paton, Christopher A. McDevitt
Abstract: Pseudomonas aeruginosa is a ubiquitous environmental bacterium and a clinically significant opportunistic human pathogen. Central to the ability of P. aeruginosa to colonise both environmental and host niches is the acquisition of zinc. Here we show that P. aeruginosa PAO1 acquires zinc via an ATP-binding cassette (ABC) permease in which ZnuA is the high affinity, zinc-specific binding protein. Zinc uptake in Gram-negative organisms predominantly occurs via an ABC permease, and consistent with this expectation a P. aeruginosa ΔznuA mutant strain showed an ~60% reduction in cellular zinc accumulation, while other metal ions were essentially unaffected. Despite the major reduction in zinc accumulation, minimal phenotypic differences were observed between the wild-type and ΔznuA mutant strains. However, the effect of zinc limitation on the transcriptome of P. aeruginosa PAO1 revealed significant changes in gene expression that enable adaptation to low-zinc conditions. Genes significantly up-regulated included non-zinc-requiring paralogs of zinc-dependent proteins and a number of novel import pathways associated with zinc acquisition. Collectively, this study provides new insight into the acquisition of zinc by P. aeruginosa PAO1, revealing a hitherto unrecognized complexity in zinc homeostasis that enables the bacterium to survive under zinc limitation.
Keywords: Bacteriology; Metalloproteins
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
RMID: 0030033254
DOI: 10.1038/srep13139
Grant ID: http://purl.org/au-research/grants/arc/DP120103957
http://purl.org/au-research/grants/nhmrc/1022240
http://purl.org/au-research/grants/nhmrc/565526
Appears in Collections:Molecular and Biomedical Science publications

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