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

  1. Lookup NU author(s)
  2. Dr Richard Jackson
  3. Dr Alison Graham
Author(s)Jackson RJ, Binet MRB, Lee LJ, Ma R, Graham AI, McLeod CW, Poole RK
Publication type Article
JournalFEMS Microbiology Letters
Year2008
Volume289
Issue2
Pages219-224
ISSN (print)0378-1097
ISSN (electronic)1574-6968
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Escherichia coli possesses two major systems for inorganic phosphate (P(i)) 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 mu M), in the absence of added P(i), 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 P(i) 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 P(i) is unknown but appears not to involve Fur or other well-characterized regulators.
PublisherWiley-Blackwell Publishing Ltd.
URLhttp://dx.doi.org/10.1111/j.1574-6968.2008.01386.x
DOI10.1111/j.1574-6968.2008.01386.x
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