Iron-Responsive Gene Regulation in a Campylobacter jejuni fur Mutant

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Journal of Bacteriology, October 1998, p. 5291-5298, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Iron-Responsive Gene Regulation in a Campylobacter jejuni fur Mutant

Arnoud H. M. van Vliet, Karl G. Wooldridge, and Julian M. Ketley^*

Department of Genetics, University of Leicester, Leicester LE1 7RH, United Kingdom

Received 20 March 1998/Accepted 5 August 1998

The expression of iron-regulated systems in gram-negative bacteria is generally controlled by the Fur protein, which repressesthe transcription of iron-regulated promoters by using Fe²⁺ as a cofactor. Mutational analysis of the Campylobacter jejunifur gene was carried out by generation of a set of mutant copiesof fur which had a kanamycin or chloramphenicol resistance geneintroduced into the regions encoding the N and C termini of theFur protein. The mutated genes were recombined into the C. jejuniNCTC 11168 chromosome, and putative mutants were confirmed bySouthern hybridization. C. jejuni mutants were obtained only whenthe resistance genes were transcribed in the same orientationas the fur gene. The C. jejuni fur mutant grew slower than theparental strain. Comparison of protein profiles of fractionatedC. jejuni cells grown in low- or high-iron medium indicated derepressedexpression of three iron-regulated outer membrane proteins withmolecular masses of 70, 75, and 80 kDa. Characterization by N-terminalamino acid sequencing showed the 75-kDa protein to be identicalto CfrA, a Campylobacter coli siderophore receptor homologue,whereas the 70-kDa protein was identified as a new siderophorereceptor homologue. Periplasmic fractions contained four derepressedproteins with molecular masses of 19, 29, 32, and 36 kDa. The19-kDa protein has been previously identified, but its functionis unknown. The cytoplasmic fraction contained two iron-repressedand two iron-induced proteins with molecular masses of 26, 55,31, and 40 kDa, respectively. The two iron-repressed proteinshave been previously identified as the oxidative stress defenseproteins catalase (KatA) and alkyl hydroperoxide reductase (AhpC).AhpC and KatA were still iron regulated in the fur mutant, suggestingthe presence of Fur-independent iron regulation. Further analysisof the C. jejuni iron and Fur regulons by using two-dimensionalgel electrophoresis demonstrated the total number of iron- andFur-regulated proteins to be lower than for other bacterial pathogens.

^* Corresponding author. Mailing address: Department of Genetics, University of Leicester, University Road, Leicester LE1 7RH,United Kingdom. Phone: 44-116-2523434. Fax: 44-116-2523378. E-mail:ket{at}le.ac.uk.

Present address: Department of Medical Microbiology, Faculty of Medicine, Vrije Universiteit Amsterdam, 1081 BT Amsterdam,The Netherlands.

Present address: Meningococcal Research Group, Division of Microbiology, University Hospital, Nottingham NG7 2UH, United Kingdom.

Journal of Bacteriology, October 1998, p. 5291-5298, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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