Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription.
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.
Woolwine
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SC
Department of Microbiology and Immunology, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1064, USA.
Sprinkle
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AB
Wozniak
D J
DJ
D002237:Carbohydrate Dehydrogenases / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D007931:Leucyl Aminopeptidase / Q000235:genetics / Q000378:metabolism*; D016296:Mutagenesis; D011401:Promoter Regions, Genetic; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D014158:Transcription, Genetic
D002237:Carbohydrate Dehydrogenases; C020562:GDPmannose dehydrogenase; D007931:Leucyl Aminopeptidase