Expression of the PitA phosphate/metal transporter of Escherichia coli is responsive to zinc and inorganic phosphate levels

Jackson, Rachel J., Binet, M. R. B., Lee, Lucy J., Ma, Renli, Graham, Alastair, McLeod, Cameron and Poole, Robert (2008) Expression of the PitA phosphate/metal transporter of Escherichia coli is responsive to zinc and inorganic phosphate levels. FEMS Microbiology Letters, 289 (2). pp. 219-224. ISSN 0378-1097

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Official URL: http://dx.doi.org/10.1111/j.1574-6968.2008.01386.x

Abstract

Escherichia coli possesses two major systems for inorganic phosphate (Pi) uptake. The Pst system (pstSCAB) is inducible by low phosphate concentrations whereas the low-affinity transporter (pitA) has been described as constitutively expressed. PitA catalyses transport of metal [Mg(II), Ca(II)]–phosphate complexes, and mutations in pitA confer Zn(II) resistance. Here we report that pitA transcription is not constitutive; activity of a single-copy pitA–lacZ transcriptional fusion (monolysogen) was maximal at high extracellular Zn(II) (150 ?M), in the absence of added Pi, and in a well-defined pitA mutant strain. Intracellular zinc levels were unaffected by adding Zn(II) to the medium for both the wild-type and mutant strains. However, in the wild-type strain, Mg levels (per gram of dry biomass) fell by eightfold in cells grown with added Zn(II) and by 20-fold when Zn(II) and Pi were added to cultures. Mutation of pitA reduced the effects of external Zn(II) and phosphate levels on Mg pools, consistent with competition or inhibition by Zn(II) of PitA. The mechanism of pitA regulation by extracellular Zn(II) and Pi is unknown but appears not to involve Fur or other well-characterized regulators.

Item Type: Article
Subjects: C500 Microbiology
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: EPrints Services
Date Deposited: 25 Feb 2010 12:46
Last Modified: 10 Aug 2015 11:46
URI: http://nrl.northumbria.ac.uk/id/eprint/473

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