Abstract
Protein ubiquitination is one of a major posttranslational modification presented in all eukaryote cells. Ubiqtuitn is attached to a substrate protein as a signal molecule to lead various outcomes, such as degradation by 26S proteasome, DNA repair and endocytosis. Ubiquitination of target proteins requires sequential actions of three enzymes; E1, E2 and E3.
To date, it has been considered that protein ubiquitination is active in male tissue although there have been quite a few information. In this study, we identified ubiquitin-related proteins from lily anther followed by determination of ortholog proteins in Arabidopsis. Now we are analyzing one protein, which is expressed in pollen.
