Abstract
As the only member of C-terminal binding protein (CtBP) family in Arabidopsis thaliana, ANGUSTIFOLIA (AN) has not only D-isomer-specific 2-hydroxy acid dehydrogenase (D2-HDH) motif which is conserved among CtBPs, but also LXCXE motif, PEST motif, cell-cycle-specific phosphorylation site and nuclear localization signal.* We carried out the comparative analysis of AN protein with authentic CtBP/BARS family, focusing on the above-mentioned AN-specific motifs which are not found in CtBPs. AN did not show ability of interaction with the C-terminal region of E1a. Moreover, AN-specific C-terminal region was found to be required for self-association. Although AN has LXCXE motif, AN did not interact with Rb in yeast two-hybrid system. Various types of mutated ANgene were constructed and the ability of complementation of the an mutation was examined for each mutated AN. Our data strongly suggest that AN has evolved different molecular function from CtBPs.
