Characterization of Phytaspase Proteolytic Activity Using Fluorogenic Peptide Substrates.

Within the subtilase family of plant proteolytic enzymes, phytaspases are distinguished by their strict substrate cleavage specificity after an aspartate residue preceded by a characteristic tripeptide amino acid motif. This type of recognition resembles that of animal apoptotic proteases, caspases. Phytaspases attract attention not only because they are critically important for the accomplishment of stress-induced death of plant cells, but also due to their ability to specifically process precursor proteins, thus generating bioactive plant peptide hormones, systemin and phytosulfokine.

Mitochondrial localization of SESN2.

SESN2 is a member of the evolutionarily conserved sestrin protein family found in most of the Metazoa species. The SESN2 gene is transcriptionally activated by many stress factors, including metabolic derangements, reactive oxygen species (ROS), and DNA-damage. As a result, SESN2 controls ROS accumulation, metabolism, and cell viability.