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Journal of Bacteriology, April 2006, p. 3134-3137, Vol. 188, No. 8
0021-9193/06/$08.00+0     doi:10.1128/JB.188.8.3134-3137.2006

Independent Regulation of MucD, an HtrA-Like Protease in Pseudomonas aeruginosa, and the Role of Its Proteolytic Motif in Alginate Gene Regulation

Lynn F. Wood and Dennis E. Ohman*

Department of Microbiology and Immunology, Virginia Commonwealth University, Medical College of Virginia Campus, Richmond, Virginia 23298-0678, and McGuire Veterans Affairs Medical Center, Richmond, Virginia 23249

Received 19 December 2005/ Accepted 9 February 2006

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.

* Corresponding author. Mailing address: Dept. of Microbiology and Immunology, Virginia Commonwealth University, Medical College of Virginia Campus, 1101 E. Marshall St., 5-047 Sanger Hall, P.O. Box 980678, Richmond, VA 23298-0678. Phone: (804) 828-9728. Fax: (804) 828-9946. E-mail: deohman{at}vcu.edu.

Journal of Bacteriology, April 2006, p. 3134-3137, Vol. 188, No. 8
0021-9193/06/$08.00+0     doi:10.1128/JB.188.8.3134-3137.2006




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