Abstract
CND41 isolated from chloroplast nucleoid of tobacco is a novel DNA binding-aspartic protease. To characterize the general function of CND41 in other plant species, we characterized the homologues in Arabidopsis. Two homologues, At5g10760 and At5g10770, showed 49% and 55% identity with CND41 on amino acid level and had conserved aspartic protease domain. However, these two genes lack the Lys-rich region unique to CND41. Then, we searched Arabidopsis genome and found another gene At2g42980 with 28% identity. We analyzed the expression pattern of these genes, At5g10770 were expressed in root and stem, whereas At5g10760 and At2g42980 showed higher expression in rosette and cauline leaf respectively. To characterize their physiological functions, we produced transgenic plants with modified expression of Arabidopsis CND41 homologues using overexpression- and RNAi-vectors. We will discuss the function of CND41 homologues in Arabidopsis with these transformants.
