Regulation of Ferritin-Mediated Cytoplasmic Iron Storage by the Ferric Uptake Regulator Homolog (Fur) of Helicobacter pylori

doi:10.1128/JB.182.21.5948-5953.2000

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Journal of Bacteriology, November 2000, p. 5948-5953, Vol. 182, No. 21
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Regulation of Ferritin-Mediated Cytoplasmic Iron Storage by the Ferric Uptake Regulator Homolog (Fur) of Helicobacter pylori

Stefan Bereswill,¹^,^* Stefan Greiner,¹ Arnoud H. M. van Vliet,² Barbara Waidner,¹ Frank Fassbinder,¹^,³ Emile Schiltz,⁴ Johannes G. Kusters,² and Manfred Kist¹

Department of Microbiology and Hygiene, Institute of Medical Microbiology and Hygiene,¹ Institute of Microbiology,³ and Institute of Organic Chemistry and Biochemistry,⁴ University of Freiburg, D-79104 Freiburg, Germany, and Faculty of Medicine, Department of Medical Microbiology, Vrije Universiteit, 1081 BT Amsterdam, The Netherlands²

Received 12 April 2000/Accepted 1 August 2000

Homologs of the ferric uptake regulator Fur and the iron storage protein ferritin play a central role in maintaining ironhomeostasis in bacteria. The gastric pathogen Helicobacter pyloricontains an iron-induced prokaryotic ferritin (Pfr) which hasbeen shown to be involved in protection against metal toxicityand a Fur homolog which has not been functionally characterizedin H. pylori. Analysis of an isogenic fur-negative mutant revealedthat H. pylori Fur is required for metal-dependent regulationof ferritin. Iron starvation, as well as medium supplementationwith nickel, zinc, copper, and manganese at nontoxic concentrations,repressed synthesis of ferritin in the wild-type strain but notin the H. pylori fur mutant. Fur-mediated regulation of ferritinsynthesis occurs at the mRNA level. With respect to the regulationof ferritin expression, Fur behaves like a global metal-dependentrepressor which is activated under iron-restricted conditionsbut also responds to different metals. Downregulation of ferritinexpression by Fur might secure the availability of free iron inthe cytoplasm, especially if iron is scarce or titrated out byothermetals.

^* Corresponding author. Mailing address: University of Freiburg, Institute of Medical Microbiology and Hygiene, Department ofMicrobiology, Hermann-Herder-Str. 11, D-79104 Freiburg, Germany.Phone: 49-761-203-6539. Fax: 49-761-203-6562. E-mail: bereswil{at}ukl.uni-freiburg.de.

Journal of Bacteriology, November 2000, p. 5948-5953, Vol. 182, No. 21
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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