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Journal of Bacteriology, May 2001, p. 2715-2723, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2715-2723.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of the Plesiomonas shigelloides Genes Encoding the Heme Iron Utilization System

D. P. Henderson,1,* E. E. Wyckoff,2 C. E. Rashidi,1 H. Verlei,1 and A. L. Oldham1

Department of Science and Mathematics, University of Texas of the Permian Basin, Odessa, Texas 79762,1 and Section of Molecular Genetics and Microbiology, The University of Texas at Austin, Austin, Texas 787122

Received 22 November 2000/Accepted 20 February 2001

Plesiomonas shigelloides is a gram-negative pathogen which can utilize heme as an iron source. In previous work, P. shigelloides genes which permitted heme iron utilization in a laboratory strain of Escherichia coli were isolated. In the present study, the cloned P. shigelloides sequences were found to encode ten potential heme utilization proteins: HugA, the putative heme receptor; TonB and ExbBD; HugB, the putative periplasmic binding protein; HugCD, the putative inner membrane permease; and the proteins HugW, HugX, and HugZ. Three of the genes, hugA, hugZ, and tonB, contain a Fur box in their putative promoters, indicating that the genes may be iron regulated. When the P. shigelloides genes were tested in E. coli K-12 or in a heme iron utilization mutant of P. shigelloides, hugA, the TonB system genes, and hugW, hugX, or hugZ were required for heme iron utilization. When the genes were tested in a hemA entB mutant of E. coli, hugWXZ were not required for utilization of heme as a porphyrin source, but their absence resulted in heme toxicity when the strains were grown in media containing heme as an iron source. hugA could replace the Vibrio cholerae hutA in a heme iron utilization assay, and V. cholerae hutA could complement a P. shigelloides heme utilization mutant, suggesting that HugA is the heme receptor. Our analyses of the TonB system of P. shigelloides indicated that it could function in tonB mutants of both E. coli and V. cholerae and that it was similar to the V. cholerae TonB1 system in the amino acid sequence of the proteins and in the ability of the system to function in high-salt medium.

* Corresponding author. Mailing address: Department of Science and Mathematics, University of Texas of the Permian Basin, 4901 E. University Blvd., Odessa, TX 79762-0001. Phone: (915) 552-2270. Fax: (915) 552-2374. E-mail: henderson_d{at}utpb.edu.

Journal of Bacteriology, May 2001, p. 2715-2723, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2715-2723.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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