Characterization of proteins interacted to 26S proteasome in Arabidopsis

Abstract

Ubiquitin(Ub)/26S proteasome pathway plays an essential housekeeping role to eliminate the proteins which are damaged or misfolded. It is also essential for aspects of cellular regulation by removing short-lived regulatory proteins as a way to fine-tune homeostasis, adapt to new environments, and redirect growth and development. The 26S proteasome consists of two multisubunit complexes, 20S core particle (CP) and 19S regulatory particle (RP). The RP contains thirteen non-ATPase subunits (RPN) and a ring of six AAA-ATPase subunits (RPT).
We reported RPT2a and RPT5a deficient mutants resulted in enlarged leaves, which are caused by accelerated endoreduplication.
To elucidate the function of AtRPT2a, we explored interacting factors with AtRPT2a by proteome analysis. Here we report the functional analyses of the candidates.