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Journal of Bacteriology, May 2001, p. 2910-2917, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2910-2917.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Expression of the Putative Siderophore Receptor Gene bfrZ Is Controlled by the Extracytoplasmic-Function Sigma Factor BupI in Bordetella bronchiseptica

Elizabeth Pradeldagger and Camille Locht*

INSERM U447, Institut Pasteur de Lille, 59019 Lille Cedex, France

Received 25 September 2000/Accepted 30 January 2001

A new gene from Bordetella bronchiseptica, bfrZ encoding a putative siderophore receptor, was identified in a Fur-repressor titration assay. A bfrZ null mutant was constructed by allelic exchange. The protein profile of this mutant is similar to that of the wild-type parent strain. The BfrZ--BfrZ+ isogenic pair was tested for utilization of 132 different siderophores as iron sources. None of these iron sources acted as a ligand for BfrZ. Translational bfrZ::phoA and transcriptional bfrZ::lacZ fusions were introduced into the B. bronchiseptica bfrZ locus. No alkaline phosphatase or beta -galactosidase activity was detected. Sequence analysis of the bfrZ upstream region revealed the presence of two tightly linked genes, bupI and bupR. Both of these genes are located downstream from a Fur-binding sequence. BupI is homologous to Escherichia coli FecI and Pseudomonas putida PupI and belongs to the family of extracytoplasmic-function sigma factors involved in transcription of genes with extracytoplasmic functions. BupR is homologous to the FecR and PupR antisigma factors and is predicted to be localized in the inner membrane. Similar to the surface signaling receptors FecA and PupB, BfrZ bears an N-terminal extension. We found that bfrZ is not transcribed when bupI and bupR are expressed at the same level. However, overexpression of bupI from a multicopy plasmid triggers bfrZ transcription, and under these conditions BfrZ was detected in membrane fractions. By analogy with the FecI-FecR-FecA and PupI-PupR-PupB systems, our data suggest that bfrZ expression is inducible by binding of the cognate ligand to BfrZ and transduction of a signal through the envelope.

* Corresponding author. Mailing address: INSERM U447, Institut Pasteur de Lille, 59019 Lille Cedex, France. Phone: (33) 3 20 87 11 51. Fax: (33) 3 20 87 11 58. E-mail: camille.locht{at}pasteur-lille.fr.

dagger Present address: INSERM CJF 9606, Faculté de Médecine, 13385 Marseille Cedex 05, France.

Journal of Bacteriology, May 2001, p. 2910-2917, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2910-2917.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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