title: Photosynthetic electron flow affects H2O2 signaling by inactivation of catalase in Chlamydomonas reinhardtii.
abstract: A specific signaling role for H(2)O(2) in Chlamydomonas reinhardtii was demonstrated by the definition of a promoter that specifically responded to this ROS. Expression of a nuclear-encoded reporter gene driven by this promoter was shown to depend not only on the level of exogenously added H(2)O(2) but also on light. In the dark, the induction of the reporter gene by H(2)O(2) was much lower than in the light. This lower induction was correlated with an accelerated disappearance of H(2)O(2) from the culture medium in the dark. Due to a light-induced reduction in catalase activity, H(2)O(2) levels in the light remained higher. Photosynthetic electron transport mediated the light-controlled down-regulation of the catalase activity since it was prevented by 3-(3'4'-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of photosystem II. In the presence of light and DCMU, expression of the reporter gene was low while the addition of aminotriazole, a catalase inhibitor, led to a higher induction of the reporter gene by H(2)O(2) in the dark. The role of photosynthetic electron transport and thioredoxin in this regulation was investigated by using mutants deficient in photosynthetic electron flow and by studying the correlation between NADP-malate dehydrogenase and catalase activities. It is proposed that, contrary to expectations, a controlled down-regulation of catalase activity occurs upon a shift of cells from dark to light. This down-regulation apparently is necessary to maintain a certain level of H(2)O(2) required to activate H(2)O(2)-dependent signaling pathways.
authors.affiliation: Fakultät für Biologie, Institut für Biologie III, Universität Freiburg, Freiburg, Germany.
authors.forename: Ning
authors.initials: N
authors.lastname: Shao
authors.forename: Christoph F
authors.initials: CF
authors.lastname: Beck
authors.forename: Stéphane D
authors.initials: SD
authors.lastname: Lemaire
authors.forename: Anja
authors.initials: A
authors.lastname: Krieger-Liszkay
mesh_terms: D020418:Algal Proteins / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism; D000640:Amitrole / Q000494:pharmacology; D000818:Animals; D002374:Catalase / Q000037:antagonists & inhibitors*; D016825:Chlamydomonas reinhardtii / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D004237:Diuron / Q000494:pharmacology; D015536:Down-Regulation; D004579:Electron Transport / Q000235:genetics / Q000502:physiology*; D005786:Gene Expression Regulation / Q000187:drug effects / Q000528:radiation effects; D017930:Genes, Reporter; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics; D006861:Hydrogen Peroxide / Q000378:metabolism* / Q000494:pharmacology; D008027:Light; D049410:Luciferases, Renilla / Q000235:genetics; D050538:Malate Dehydrogenase (NADP+) / Q000378:metabolism / Q000502:physiology; D009154:Mutation; D010084:Oxidation-Reduction; D010788:Photosynthesis / Q000235:genetics / Q000502:physiology*; D011401:Promoter Regions, Genetic; D012333:RNA, Messenger / Q000378:metabolism; D015398:Signal Transduction; D013879:Thioredoxins / Q000502:physiology
chemical_list: D020418:Algal Proteins; D018840:HSP70 Heat-Shock Proteins; D012333:RNA, Messenger; D013879:Thioredoxins; D004237:Diuron; D006861:Hydrogen Peroxide; D050538:Malate Dehydrogenase (NADP+); D002374:Catalase; D049410:Luciferases, Renilla; D000640:Amitrole
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