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.
Wood
Lynn F
LF
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.
Ohman
Dennis E
DE
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