title: The dsbA-dsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance.
abstract: In a previous study, we isolated a dsbB mutant of Burkholderia cepacia KF1 and showed that phenotypes of protease production and motility are dependent on DsbB, a membrane-bound disulfide bond oxidoreductase. We have now isolated a dsbA mutant by transposon mutagenesis, cloned the dsbA gene encoding a periplasmic disulfide bond oxidoreductase, and characterized the function of the DsbA-DsbB disulfide bond formation system in B. cepacia. The complementing DNA fragment had an open reading frame for a 212-amino acid polypeptide with a potential redox-active site sequence of Cys-Pro-His-Cys that is homologous to Escherichia coli DsbA. The dsbA mutant, as well as the previously isolated dsbB mutant, was defective in the production of extracellular protease and alkaline phosphatase, as well as in motility. In addition, mutation in the DsbA-DsbB system resulted in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate. These results suggested that the DsbA-DsbB system might be involved in the formation of a metal efflux system as well as a multi-drug resistance system.
authors.affiliation: Department of Microbiology, Yamaguchi University School of Medicine, Ube, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Hayashi
authors.forename: M
authors.initials: M
authors.lastname: Abe
authors.forename: M
authors.initials: M
authors.lastname: Kimoto
authors.forename: S
authors.initials: S
authors.lastname: Furukawa
authors.forename: T
authors.initials: T
authors.lastname: Nakazawa
mesh_terms: D000469:Alkaline Phosphatase / Q000096:biosynthesis; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D016956:Burkholderia cepacia / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004220:Disulfides; D004352:Drug Resistance, Microbial; D018432:Drug Resistance, Multiple; D010450:Endopeptidases / Q000096:biosynthesis; D005798:Genes, Bacterial; D007769:Lactams / Q000494:pharmacology; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019216:Metals, Heavy / Q000494:pharmacology; D008969:Molecular Sequence Data; D009068:Movement; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D019895:Transposases
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004220:Disulfides; C079503:DsbB protein, Bacteria; D007769:Lactams; D008565:Membrane Proteins; D019216:Metals, Heavy; D010088:Oxidoreductases; D019895:Transposases; D000469:Alkaline Phosphatase; D010450:Endopeptidases; D019704:Protein Disulfide-Isomerases