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Molecular and cellular characterisation of the zinc uptake (Znu) system of Nostoc punctiforme

Hudek, Lee, Pearson, Leanne A., Michalczyk, Agnes, Neilan, Brett A. and Ackland, M. Leigh 2013, Molecular and cellular characterisation of the zinc uptake (Znu) system of Nostoc punctiforme, FEMS microbiology ecology, vol. 86, no. 2, pp. 149-171, doi: 10.1111/1574-6941.12153.

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Title Molecular and cellular characterisation of the zinc uptake (Znu) system of Nostoc punctiforme
Author(s) Hudek, LeeORCID iD for Hudek, Lee orcid.org/0000-0002-5722-9346
Pearson, Leanne A.
Michalczyk, AgnesORCID iD for Michalczyk, Agnes orcid.org/0000-0001-5716-0783
Neilan, Brett A.
Ackland, M. LeighORCID iD for Ackland, M. Leigh orcid.org/0000-0002-7474-6556
Journal name FEMS microbiology ecology
Volume number 86
Issue number 2
Start page 149
End page 171
Total pages 23
Publisher Wiley-Blackwell
Place of publication Oxford, England
Publication date 2013
ISSN 0168-6496
1574-6941
Keyword(s) heavy metals
metal transporters
nostoc punctiforme
zinc
Summary Metal homoeostasis in cyanobacteria is based on uptake and export systems that are controlled by their own regulators. This study characterises the zinc uptake (Znu) system in Nostoc punctiforme. The system was found to comprise of three subunits in an ACB operon: a Zn2+-binding protein (ZnuA18), a transmembrane domain (ZnuB) and an ATPase (ZnuC). These proteins are encoded within the znu operon regulated by a zinc uptake transcription repressor (Zur). Interestingly, a second Zn2+-binding protein (ZnuA08) was also identified at a distal genomic location. Interactions between components of the ZnuACB system were investigated using knockouts of the individual genes. The znuA08-, znuA18-, znuB- and znuC- mutants displayed overall reduced znuACB transcript levels, suggesting that all system components are required for normal expression of znu genes. Zinc uptake assays in the Zn2+-binding protein mutant strains showed that the disruption of znuA18 had a greater negative effect on zinc uptake than disruption of znuA08. Complementation studies in Escherichia coli indicated that both znuA08 and znuA18 were able to restore zinc uptake in a znuA- mutant, with znuA18 permitting the highest zinc uptake rate. The N. punctiforme zur was also able to complement the E. coli zur- mutant.
Language eng
DOI 10.1111/1574-6941.12153
Field of Research 059999 Environmental Sciences not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Persistent URL http://hdl.handle.net/10536/DRO/DU:30055268

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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Created: Tue, 27 Aug 2013, 11:49:18 EST

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