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Functional characterization of the twin ZIP/SLC39 metal transporters, NpunF3111 and NpunF2202 in Nostoc punctiforme

Hudek, L., Pearson, L.A., Michalczyk, A., Neilan, B.A. and Ackland, M.L. 2013, Functional characterization of the twin ZIP/SLC39 metal transporters, NpunF3111 and NpunF2202 in Nostoc punctiforme, Applied microbiology and biotechnology, vol. 97, no. 19, pp. 8649-8662, doi: 10.1007/s00253-013-5047-y.

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Title Functional characterization of the twin ZIP/SLC39 metal transporters, NpunF3111 and NpunF2202 in Nostoc punctiforme
Author(s) Hudek, L.ORCID iD for Hudek, L. orcid.org/0000-0002-5722-9346
Pearson, L.A.
Michalczyk, A.ORCID iD for Michalczyk, A. orcid.org/0000-0001-5716-0783
Neilan, B.A.
Ackland, M.L.ORCID iD for Ackland, M.L. orcid.org/0000-0002-7474-6556
Journal name Applied microbiology and biotechnology
Volume number 97
Issue number 19
Start page 8649
End page 8662
Total pages 14
Publisher Springer
Place of publication Berlin, Germany
Publication date 2013
ISSN 0175-7598
1432-0614
Keyword(s) cyanobacteria
divalent cation
metal transport
SLC39
zinc uptake
ZIP
Summary The ZIP family of metal transporters is involved in the transport of Zn2+ and other metal cations from the extracellular environment and/or organelles into the cytoplasm of prokaryotes, eukaryotes and archaeotes. In the present study, we identified twin ZIP transporters, Zip11 (Npun_F3111) and Zip63 (Npun_F2202) encoded within the genome of the filamentous cyanobacterium, Nostoc punctiforme PCC73120. Sequence-based analyses and structural predictions confirmed that these cyanobacterial transporters belong to the SLC39 subfamily of metal transporters. Quantitative real-time (QRT)-PCR analyses suggested that the enzymes encoded by zip11 and zip63 have a broad allocrite range that includes zinc as well as cadmium, cobalt, copper, manganese and nickel. Inactivation of either zip11 or zip63 via insertional mutagenesis in N. punctiforme resulted in reduced expression of both genes, highlighting a possible co-regulation mechanism. Uptake experiments using 65Zn demonstrated that both zip mutants had diminished zinc uptake capacity, with the deletion of zip11 resulting in the greatest overall reduction in 65Zn uptake. Over-expression of Zip11 and Zip63 in an E. coli mutant strain (ZupT736::kan) restored divalent metal cation uptake, providing further evidence that these transporters are involved in Zn uptake in N. punctiforme. Our findings show the functional role of these twin metal uptake transporters in N. punctiforme, which are independently expressed in the presence of an array of metals. Both Zip11 and Zip63 are required for the maintenance of homeostatic levels of intracellular zinc N. punctiforme, although Zip11 appears to be the primary zinc transporter in this cyanobacterium, both ZIP's may be part of a larger metal uptake system with shared regulatory elements.
Language eng
DOI 10.1007/s00253-013-5047-y
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
Copyright notice ©2013, Springer
Persistent URL http://hdl.handle.net/10536/DRO/DU:30055267

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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