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 Previous Article

Journal of Bacteriology, August 2001, p. 4674-4679, Vol. 183, No. 15
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.15.4674-4679.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Loss of Pseudomonas aeruginosa PhpA Aminopeptidase Activity Results in Increased algD Transcription

Samuel C. Woolwine,dagger April B. Sprinkle, and Daniel J. Wozniak*

Department of Microbiology and Immunology, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157-1064

Received 20 October 2000/Accepted 11 May 2001

Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algD transcription initiation site and was not due to activation of an alternative promoter.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1064. Phone: (336) 716-2016. Fax: (336) 716-9928. E-mail: dwozniak{at}wfubmc.edu.

dagger Present address: Departments of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Journal of Bacteriology, August 2001, p. 4674-4679, Vol. 183, No. 15
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.15.4674-4679.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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