Arabidopsis GLYCOLATE OXIDASE 1 and 2 display divergent roles under conditions promoting photorespiration

ABSTRACT: Hydrogen peroxide (H2O2) can act as a signaling molecule that influences various aspects of plant growth and development, including stress signaling and cell death. To unravel the molecular mechanisms that regulate the response towards an impact of increased H2O2 levels in plant cells, we focused on the photorespiration-dependent peroxisomal H2O2 production in Arabidopsis thaliana mutants lacking CATALASE2 (CAT2) activity (cat2-2) and screened for second-site mutations that attenuate the Fv'/Fm' decrease and lesion formation linked to the cat2-2 phenotype. A mutation in GLYCOLATE OXIDASE 1, encoding one of the two photorespiratory isoforms of glycolate oxidase rescued the cell death phenotype of cat2-2 plants under photorespiration-promoting conditions. Interestingly, introduction of gox2 into the cat2 background did not have the same effect and the double cat2 gox2 mutants were as affected as the parental cat2 mutants under conditions promoting photorespiration. Using a series of physiological, biochemical and metabolomic approaches we investigated the differential photorespiratory response of cat2 mutants underlied by the lack of GOX1 and GOX2. These differences are in line with the non-redundant functions of GOX1 and GOX2 which could be observed under enhanced photorespiration. Unstressed and stressed samples of cat2 gox1 and cat2 gox2 double mutants in triplicate

ORGANISM(S): Arabidopsis thaliana

SUBMITTER: Patrick Willems 

PROVIDER: E-GEOD-77170 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress