Abstract
Ubiquitylation is one of major modifications of proteins, which is highly conserved in all eukaryote. Ubiquitination is a signal to be degraded for short-termed and misfolded proteins by 26 S proteasome. In addition, several proteins are ubiquitinated for their regulation in endocytosis, signal transduction and DNA repair. Recently, proteome analysis of the ubiquitinated proteins have been reported in yeast and mammal, however, there is less information in higher plants. Thus, we aim to clarify the ubiquitinated proteins in Arabidopsis thaliana by proteome analysis.
We purified the ubiquitinated proteins using a NHS-activated column coupled with anti-ubiquitin antibody, and identified their proteins by LC-MS/MS analysis. Here we report the candidates of ubiquitinated proteins in Arabidopsis.
