Work

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

Year: 2001

Type: article

Abstract: 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.

Source: Journal of Bacteriology

DOI: 10.1128/jb.183.15.4674-4679.2001

Authors: Samuel C. Woolwine, April B. Sprinkle, Daniel J. Wozniak

Institutions: Wake Forest University Health Sciences, Wake Forest University

Language: English

Topic: Bacterial biofilms and quorum sensing

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Heart, Lung, and Blood Institute, National Institute of Allergy and Infectious Diseases

Awards: G5200406502, Control of P. aeruginosa algD transcription, G759337113