Abstract
26S proteasome is a large multisubunit complex that degrades aberrant cellular proteins. Most subunits of plant proteasome are coded by duplicated genes. However, specific functions of each paralogous subunit remain unclear. We have revealed that loss-of-function mutant of proteasome palalog shows different response to nutrient stress, suggesting each palalog has different functions.
Furthermore, it has been reported that peptidase activities of proteasome are altered responding to nutrient and oxidative stress. These results suggest that peptidase activities of plant proteasome are important in response to environmental stress.
To evaluate this hypothesis, we tried to detect alteration of peptidase activities and structural transformation.
We established affinity purification of proteasome from Arabidopsis and identification of each palalog using 2-DE/MS analysis. Change in peptidase activities under varies stress conditions will be reported.
