Independent Regulation of MucD, an HtrA-Like Protease in Pseudomonas aeruginosa , and the Role of Its Proteolytic Motif in Alginate Gene Regulation
| Autor: | Dennis E. Ohman, Lynn F. Wood |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Proteases
Alginates Operon medicine.medical_treatment Genetics and Molecular Biology medicine.disease_cause Microbiology Bacterial Proteins Glucuronic Acid medicine Promoter Regions Genetic Molecular Biology Gene Regulation of gene expression Protease biology Pseudomonas aeruginosa Hexuronic Acids Serine Endopeptidases Gene Expression Regulation Bacterial biology.organism_classification Amino Acid Substitution Mutation Pseudomonadales Pseudomonadaceae |
| Zdroj: | Journal of Bacteriology. 188:3134-3137 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.188.8.3134-3137.2006 |
| Popis: | 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 (P mucD ) 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. |
| Databáze: | OpenAIRE |
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