Molecular Mechanisms of Bacterial Virulence pp 491-504 | Cite as
Regulation of the iron transport genes encoded by the pJM1 virulence plasmid in Vibrio anguillarum
Abstract
An important component of the virulence of Vibrio anguillarum 775 is the pJMl plasmid-mediated iron uptake system which consists of the siderophore anguibactin and the iron transport proteins FatA-D. Expression of this system is repressed when the iron concentration of the cell is high. We have now shown that under iron-rich conditions two elements may a play a role in the control of the expression of the fat A gene: a Fur-like product and a 600 nucleotides antisense RNA, RNAα, which is encoded in the fatA-fatB intergenic region and is induced at high iron concentrations. Under iron-limiting conditions two positive regulators, Taf and AngR, are necessary for full expression of the siderophore biosynthetic genes. AngR, a 110 kDa protein, possesses two helix-turn-helix domains with adjacent leucine zippers that may play a role in the regulatory activity of this protein as assessed by site-directed mutagenesis. We have also identified a novel catalytic activity of AngR suggesting that, in addition to its regulatory role, it acts as an enzyme in the biosynthesis of anguibactin.
Keywords
Leucine Zipper Iron Transport Vibrio Anguillarum Iron Uptake System Total Membrane ProteinAbbreviations
- AMP
Adenosme Monophoshate
- EDDA
Ethylenediamine-di Co-hydroxyphenyla-cetic Acid
- MIC
Minimal Inhibitory Concentration
- SDS-page
Sodium Dodecyl Salphate-Poly Acrylamide Gel Electrophorhesis
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References
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