Siderophore activity of myo-inositol hexakisphosphate in Pseudomonas aeruginosa

Anthony W. Smith, David R. Poyner, H.K. Hughes, Peter A. Lambert

Research output: Contribution to journalArticle

Abstract

Myo-Inositol hexakisphosphate (InsP6), which is found in soil and most, if not all, plant and animal cells, has been estimated to have an affinity for Fe3+ in the range of 10(25) to 10(30) M-1. In this report, we demonstrate that the Fe-InsP6 complex has siderophore activity and is able to reverse the iron-restricted growth inhibition of Pseudomonas aeruginosa by ethylene diamine di(o-hydroxyphenyl)acetic acid. With 55Fe-InsP6 in transport studies, iron uptake is strongly iron regulated, being repressed after growth in iron-replete conditions and inhibited by treatment with potassium cyanide and carbonyl cyanide m-chlorophenylhydrazone. The kinetics of iron transport revealed a Km of 100 nM. Self-displacement of binding of [3H]InsP6 to isolated membranes by InsP6 revealed a single class of binding sites (Kd = 143 +/- 6 nM; Hill coefficient, 1.1 +/- 0.1). The binding of [3H]InsP6 to membranes was not dependent on whether cells had been grown under conditions of high or low iron concentrations. We believe that this is the first report of inositol polyphosphate activity in prokaryotic cells.
Original languageEnglish
Pages (from-to)3455-3459
Number of pages5
JournalJournal of Bacteriology
Volume176
Issue number12
DOIs
Publication statusPublished - 14 Jun 1994

Fingerprint

Siderophores
Phytic Acid
Pseudomonas aeruginosa
Iron
Potassium Cyanide
Prokaryotic Cells
Polyphosphates
Diamines
Membranes
Plant Cells
Inositol
Growth
Soil
Binding Sites

Keywords

  • binding
  • competitive
  • cell division
  • cell membrane
  • dose-response relationship
  • drug
  • ferric compounds
  • iron phytic acid
  • pseudomonas aeruginosa
  • siderophores
  • time factors

Cite this

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title = "Siderophore activity of myo-inositol hexakisphosphate in Pseudomonas aeruginosa",
abstract = "Myo-Inositol hexakisphosphate (InsP6), which is found in soil and most, if not all, plant and animal cells, has been estimated to have an affinity for Fe3+ in the range of 10(25) to 10(30) M-1. In this report, we demonstrate that the Fe-InsP6 complex has siderophore activity and is able to reverse the iron-restricted growth inhibition of Pseudomonas aeruginosa by ethylene diamine di(o-hydroxyphenyl)acetic acid. With 55Fe-InsP6 in transport studies, iron uptake is strongly iron regulated, being repressed after growth in iron-replete conditions and inhibited by treatment with potassium cyanide and carbonyl cyanide m-chlorophenylhydrazone. The kinetics of iron transport revealed a Km of 100 nM. Self-displacement of binding of [3H]InsP6 to isolated membranes by InsP6 revealed a single class of binding sites (Kd = 143 +/- 6 nM; Hill coefficient, 1.1 +/- 0.1). The binding of [3H]InsP6 to membranes was not dependent on whether cells had been grown under conditions of high or low iron concentrations. We believe that this is the first report of inositol polyphosphate activity in prokaryotic cells.",
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Siderophore activity of myo-inositol hexakisphosphate in Pseudomonas aeruginosa. / Smith, Anthony W.; Poyner, David R.; Hughes, H.K.; Lambert, Peter A.

In: Journal of Bacteriology, Vol. 176, No. 12, 14.06.1994, p. 3455-3459.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Siderophore activity of myo-inositol hexakisphosphate in Pseudomonas aeruginosa

AU - Smith, Anthony W.

AU - Poyner, David R.

AU - Hughes, H.K.

AU - Lambert, Peter A.

PY - 1994/6/14

Y1 - 1994/6/14

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AB - Myo-Inositol hexakisphosphate (InsP6), which is found in soil and most, if not all, plant and animal cells, has been estimated to have an affinity for Fe3+ in the range of 10(25) to 10(30) M-1. In this report, we demonstrate that the Fe-InsP6 complex has siderophore activity and is able to reverse the iron-restricted growth inhibition of Pseudomonas aeruginosa by ethylene diamine di(o-hydroxyphenyl)acetic acid. With 55Fe-InsP6 in transport studies, iron uptake is strongly iron regulated, being repressed after growth in iron-replete conditions and inhibited by treatment with potassium cyanide and carbonyl cyanide m-chlorophenylhydrazone. The kinetics of iron transport revealed a Km of 100 nM. Self-displacement of binding of [3H]InsP6 to isolated membranes by InsP6 revealed a single class of binding sites (Kd = 143 +/- 6 nM; Hill coefficient, 1.1 +/- 0.1). The binding of [3H]InsP6 to membranes was not dependent on whether cells had been grown under conditions of high or low iron concentrations. We believe that this is the first report of inositol polyphosphate activity in prokaryotic cells.

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