4.4 Article

Independent regulation of MucD, an HtrA-like protease in Pseudomonas aeruginosa, and the role of its proteolytic motif in alginate gene regulation

Journal

JOURNAL OF BACTERIOLOGY
Volume 188, Issue 8, Pages 3134-3137

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.188.8.3134-3137.2006

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Funding

  1. NIAID NIH HHS [R56 AI019146, AI 19146, R01 AI019146] Funding Source: Medline

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Expression of mucD, encoding a homologue of the HtrA(DegP) family of endoserine proteases, was investigated in Pseudomonas aeruginosa. Expressed from the algT-mucABCD operon, MucD was detected in mucoid (FRD1) and nonmucoid (PAO1) parental strains and also when polar insertions were placed upstream in algT or mucB. A transcriptional start site for a mucD promoter (PmucD) was mapped within mucC. Expression of single-copy mucD217, encoding MucD altered in the protease motif (S217A), was defective in temperature resistance and alginate gene regulation.

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