Arabidopsis Iron Superoxide Dismutase FSD1 Protects Against Methyl Viologen-Induced Oxidative Stress in a Copper-Dependent Manner

• DOI: 10.3389/fpls.2022.823561
• Publication Date: 2022-03-11T10:34:16Z
• Authors: Pavol Melicher; Petr Dvořák; Yuliya Krasylenko; Alexey Shapiguzov; Jaakko Kangasjärvi; Jozef Šamaj; Tomáš Takáč
• Keywords: 570; HOMEOSTASIS; PROTEINS; Arabidopsis; Plant Science; OXYGEN; SB1-1110; 03 medical and health sciences; proteomics; CHLOROPLASTS; oxidative stress; PLANTS; TOLERANCE; methyl viologen; Biochemistry, cell and molecular biology; 0303 health sciences; PHOTOSYNTHESIS; ta1183; Plant culture; PARAQUAT; 11831 Plant biology; ferredoxin; superoxide dismutase; 620; FSD1; copper; GROWTH; REDOX PROTEOMICS

Iron superoxide dismutase 1 (FSD1) was recently characterized as a plastidial, cytoplasmic, and nuclear enzyme with osmoprotective antioxidant functions. However, the current knowledge on its role in oxidative stress tolerance is ambiguous. Here, we of FSD1 response to methyl viologen (MV)-induced Arabidopsis thaliana. In accordance known regulation expression, abundance, activity, findings demonstrated that function depends availability Cu2+ growth media. fsd1 mutants showed lower capacity decompose at low concentrations medium. Prolonged exposure MV led reduced ascorbate levels higher protein carbonylation transgenic plants lacking plastid pool compared wild type. induced rapid increase followed by decrease after 4 h long exposure. Genetic disruption negatively affected hydrogen peroxide-decomposing peroxidase mutants. Chloroplastic localization crucial maintain redox homeostasis. Proteomic analysis sensitivity coincided decreased abundances ferredoxin photosystem II light-harvesting complex proteins. These have chloroplastic proteases indicating an altered turnover chloroplasts. Moreover, affects abundance proteins involved defense response. Collectively, study provides evidence for conditional antioxidative possible signaling.