Abstract
The ERF-associated amphiphilic repression (EAR) motif is a plant specific repression domain (RD). The minimum core sequence is 6 amino acids and it acts as a repressor when fused with heterologous DNA binding domain. However, the mechanism of repression via EAR-motif (RD) is not known and it should be clarified whether a plant specific mechanism of transcriptional repression may exist. We attempted iTRAQ proteome analyses to identify factor(s) that interact with RD, and found that plant specific histone deacetylases, a histone demethylase and several nuclear proteins of unknown function were isolated. We are analyzing protein-protein interactions between these factors and RD, respectively, both in yeast and in vitro system. A sub-nuclear localization of representative proteins is examined by confocal microscopy. We present genetic evidences, that the nuclear protein involves in the RD related repression, using transgenic Arabidopsis and mutant lines. We will discuss a possible mechanism of transcriptional repression caused by the RD, including changes of histone codes, such as acethylation and methylation.
