Independent regulation of MucD, an HtrA-like protease in Pseudomonas aeruginosa, and the role of its proteolytic motif in alginate gene regulation.
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.
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, USA.
Lynn F
LF
Wood
Dennis E
DE
Ohman
D000464:Alginates; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D020723:Glucuronic Acid / Q000096:biosynthesis; D006603:Hexuronic Acids; D009154:Mutation; D011401:Promoter Regions, Genetic; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D000464:Alginates; D001426:Bacterial Proteins; D006603:Hexuronic Acids; D020723:Glucuronic Acid; C097649:MucD protein, Pseudomonas aeruginosa; D012697:Serine Endopeptidases