Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response.

We present evidence that heterotrimeric G protein signaling is involved in cell death associated with the unfolded protein response (UPR) in Arabidopsis. Seedlings of homozygous agb1-2 (Gbeta-null mutation) mutant plants are markedly more resistant to growth inhibition by the protein glycosylation inhibitor tunicamycin (Tm) than either wild-type plants or gpa1-4 (Galpha-null mutation) mutants. Leaves of older Gbeta mutant plants show much less cell death when infiltrated with Tm than leaves of wild-type plants.

The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development.

Ascorbate peroxidase (APX) exists as several isoforms that are found in various compartments in plant cells. The cytosolic and chloroplast APXs appear to play important roles in antioxidation metabolism in plant cells, yet the function of peroxisomal APX is not well studied. In this study, the localization of a putative peroxisomal membrane-bound ascorbate peroxidase, APX3 from Arabidopsis, was confirmed by studying the green fluorescent protein (GFP)-APX3 fusion protein in transgenic plants.