title: Oxidative stress in Synechococcus sp. strain PCC 7942: various mechanisms for H2O2 detoxification with different physiological roles.
abstract: This study focuses on the mechanisms for hydrogen peroxide detoxification in Synechococcus sp. strain PCC 7942. To gain better understanding of the role of different routes of hydrogen peroxide detoxification, we inactivated TplA (thioredoxin-peroxidase-like), which we recently identified. In addition, we inactivated the gene encoding catalase-peroxidase and examined the ability to detoxify H(2)O(2) and to survive oxidative stress in both of the single mutants and in the double mutant. Surprisingly, we observed that the double mutant survived H(2)O(2) concentrations that the single catalase-peroxidase mutant could not tolerate. This phenotype correlated with an increased ability of the double mutant to detoxify externally added H(2)O(2) compared to the catalase-peroxidase mutant. Therefore, our studies suggested the existence of a hydrogen peroxide detoxification activity in addition to catalase-peroxidase and thioredoxin-peroxidase. The rate of detoxification of externally added H(2)O(2) was similar in the wild-type and the TplA mutant cells, suggesting that, under these conditions, catalase-peroxidase activity was essential for this process and TplA was dispensable. However, during excessive radiation, conditions under which the cell might experience oxidative stress, TplA appears to be essential for growth, and cells lacking it cannot compete with the wild-type strain. Overall, these studies suggested different physiological roles for various cellular hydrogen peroxide detoxification mechanisms in Synechococcus sp. strain PCC 7942.
authors.affiliation: Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.
authors.forename: Alexander
authors.initials: A
authors.lastname: Perelman
authors.forename: Avraham
authors.initials: A
authors.lastname: Uzan
authors.forename: Dalia
authors.initials: D
authors.lastname: Hacohen
authors.forename: Rakefet
authors.initials: R
authors.lastname: Schwarz
mesh_terms: D002374:Catalase / Q000737:chemistry / Q000235:genetics; D000458:Cyanobacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism* / Q000494:pharmacology; D008658:Inactivation, Metabolic; D008969:Molecular Sequence Data; D009154:Mutation; D018384:Oxidative Stress; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics; D013997:Time Factors
chemical_list: D013879:Thioredoxins; D006861:Hydrogen Peroxide; D010544:Peroxidases; D002374:Catalase