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

AUTOR(ES)

Woolwine, Samuel C.

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Pseudomonas aeruginosa AlgB, a two-component response regulator of the NtrC family, is required for algD transcription.
• High osmolarity is a signal for enhanced algD transcription in mucoid and nonmucoid Pseudomonas aeruginosa strains.
• Gene algD coding for GDPmannose dehydrogenase is transcriptionally activated in mucoid Pseudomonas aeruginosa.
• Integration host factor and sequences downstream of the Pseudomonas aeruginosa algD transcription start site are required for expression.
• Pseudomonas aeruginosa infection in cystic fibrosis: nucleotide sequence and transcriptional regulation of the algD gene.