Abstract
SUMO (Small ubiquitin-related modifier) is a member of the superfamily of ubiquitin-related polypeptides that become covalently attached to various intracellular target proteins as a way to alter their function, location, and/or half-life. Arabidopsis thaliana has 8 SUMO genes (AtSUMO1-8), which are suggested to have individual function. Expression analysis using the GUS reporter gene revealed the tissue specific expression pattern of each SUMO gene. We are now investigating the processing of C terminus, the ability of Sumoylation and the target specificity of each SUMO isoform. Moreover, it was reported that SUMO could convert the protein function through the non-covalent interaction with the target proteins. Since the Gly-Gly motif, which is necessary for the covalent modification, is not conserved in AtSUMO4, 6 and 7, they might function in the protein conformation change through the possible non-covalent interaction with their target proteins.
