Abstract
Protein ubiquitination and degradation are key processes in the development of eukaryotes and their various physiological responses. Skp1 forms SCF E3 ligase with Cullin1, F-box protein, and RBX1 to catalyze protein ubiquitination in co-operation with enzymes E1 and E2. In Arabidopsis thaliana, there are 21 Skp1-like (ASK) genes. ASK20 has two translational products, ASK20A and ASK20B, due to variation in splicing. These deduced proteins have four helix domains at their N-termini, which bind with F-box motif and are conserved in all ASK proteins, while they also have functionally unknown regions at their C-termini, which are absent in other ASK proteins. In this study, we performed several fundamental characterizations of ASK20 to understand its function. In addition, possible functions of ASK20A and ASK20B will be discussed.
This work was supported by a grant from the Program for Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN).
