Abstract
Ubiquitination is one of the most prevalent post-translational modifications. Ubiquitin (Ub) share a common fold, and their transfer to the target protein is accomplished through the sequential action of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (UBE2), and a ubiquitin-protein ligase (E3). UBE2s accept a Ub from the E1 and typically interact with an E3 to promote Ub transfer to the target. All UBE2 share a ~150 residue conserved catalytic core domain. Although their three-dimensional structures have been reported, the recognition mechanisms between UBE2 and E3 are not completely clarified. UBE2 isoform that exceeds 20 kinds exists also in the rice plant. We have determined that the interaction between the RING-H2 finger domain of the EL5 protein, which is rapidly induced by N-acethylchitooligosaccharides, and OsUBE2D, which is one of Rice UBE2 isoform, at an atomic level. From the results, the correlation of the structure and the function of UBE2 will be reported.
