title: The significance of type II and PrxQ peroxiredoxins for antioxidative stress response in the purple bacterium Rhodobacter sphaeroides.
abstract: Two peroxiredoxins, classified as Type II and PrxQ, were characterized in the purple non-sulfur photosynthetic bacterium Rhodobacter sphaeroides. Both recombinant proteins showed remarkable thioredoxin-dependent peroxidase activity with broad substrate specificity in vitro. Nevertheless, PrxQ of R. sphaeroides, unlike typical PrxQs studied to date, does not contain one of the two conserved catalytic Cys residues. We found that R. sphaeroides PrxQ and other PrxQ-like proteins from several organisms conserve a different second Cys residue, indicating that these proteins should be categorized into a novel PrxQ subfamily. Disruption of either the Type II or PrxQ gene in R. sphaeroides had a dramatic effect on cell viability when the cells were grown under aerobic light or oxidative stress conditions created by exogenous addition of reactive oxygen species to the medium. Growth rates of the mutants were significantly decreased compared with that of wild type under aerobic but not anaerobic conditions. These results indicate that the peroxiredoxins are crucial for antioxidative stress response in this bacterium. The gene disruptants also demonstrated reduced levels of photopigment synthesis, suggesting that the peroxiredoxins are directly or indirectly involved in regulated synthesis of the photosynthetic apparatus.
authors.affiliation: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Wakita
authors.forename: Shinji
authors.initials: S
authors.lastname: Masuda
authors.forename: Ken
authors.initials: K
authors.lastname: Motohashi
authors.forename: Toru
authors.initials: T
authors.lastname: Hisabori
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Ohta
authors.forename: Ken-ichiro
authors.initials: K
authors.lastname: Takamiya
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial; D016680:Genome, Bacterial; D007700:Kinetics; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010100:Oxygen / Q000378:metabolism; D010544:Peroxidases / Q000737:chemistry / Q000502:physiology*; D054464:Peroxiredoxins; D012242:Rhodobacter sphaeroides / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D013438:Sulfhydryl Compounds; D010544:Peroxidases; D054464:Peroxiredoxins; D003545:Cysteine; D010100:Oxygen