title: Chilling stress and mitochondrial genome rearrangement in the MSC16 cucumber mutant affect the alternative oxidase and antioxidant defense system to a similar extent.
abstract: The mosaic MSC16 cucumber (Cucumis sativus L.) mutant, which houses a rearranged mitochondrial genome, has altered respiratory chain activity, with a dysfunctional Complex I, increased external NADH dehydrogenases (ND(ex)) activity, and a higher alternative oxidase (AOX) capacity and AOX protein level. In the present study, changes in oxidative defense metabolism resulting from the respiratory chain dysfunction in the MSC16 mutant were compared with those induced by chilling. Chilling increased the enzymatic and non-enzymatic antioxidant defense systems in the wild-type (WT) but not in MSC16, which displays elevated antioxidant defenses as a result of the mitochondrial mutation. The high AOX capacity and protein level in MSC16 were unchanged as a result of chilling, whereas chilling increased these parameters in WT leaves. In mitochondria isolated from WT plants, superoxide was produced to a similar extent in the matrix and the intermembrane space, but in MSC16 mitochondria superoxide was produced largely within the intermembrane space. Mitochondria isolated from both genotypes after chilling showed increased superoxide production within the intermembrane space. Cytochemical detection revealed an increased abundance of H2O2 in the mitochondrial membrane in mesophyll cells of MSC16 leaves. The mitochondrial mutation also resulted in changes in the antioxidative defense system, including AOX, which were similar to those observed following chilling. The results presented here support the hypothesis that AOX is an effective marker of the cellular reprogramming resulting from stress. Moreover, we propose a role for reactive oxygen species (ROS) generated within the mitochondria in signal transduction.
authors: Faculty of Biology, Institute of Experimental Plant Biology, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland. szal@biol.uw.edu.pl
authors: Bozena
authors: B
authors: Szal
authors: Katarzyna
authors: K
authors: Lukawska
authors: Izabela
authors: I
authors: Zdolińska
authors: Anna M
authors: AM
authors: Rychter
mesh_terms: D000975:Antioxidants / Q000378:metabolism*; D001205:Ascorbic Acid / Q000378:metabolism; D019069:Cell Respiration; D018553:Cucumis sativus / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D005615:Freezing; D015321:Gene Rearrangement / Q000235:genetics*; D054629:Genome, Mitochondrial / Q000235:genetics*; D005978:Glutathione / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D015151:Immunoblotting; D008928:Mitochondria / Q000378:metabolism / Q000648:ultrastructure; D024101:Mitochondrial Proteins; D009154:Mutation / Q000235:genetics*; D010088:Oxidoreductases / Q000378:metabolism*; D009195:Peroxidase / Q000378:metabolism; D010936:Plant Extracts / Q000378:metabolism; D018515:Plant Leaves / Q000166:cytology / Q000201:enzymology / Q000235:genetics; D010940:Plant Proteins; D013312:Stress, Physiological / Q000235:genetics; D013482:Superoxide Dismutase / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism; D000099188:Alternative Oxidase
chemical_list: D000975:Antioxidants; D001205:Ascorbic Acid; D005978:Glutathione; D006861:Hydrogen Peroxide; D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D009195:Peroxidase; D010936:Plant Extracts; D010940:Plant Proteins; D013482:Superoxide Dismutase; D013481:Superoxides; D000099188:Alternative Oxidase; C121048:guaiacol peroxidase