Research Description

Structure and mechanism of action of ribonuclease P, a catalytic ribonucleoprotein (RNP) complex. The endoribonuclease RNase P is a ubiquitous RNP that is involved in the maturation of tRNAs. In Escherichia coli, the RNase P holoenzyme consists of a catalytic RNA subunit (M1 RNA, 377 nts) and a protein cofactor (C5 protein, 119 amino acid residues). The long-term goal of our studies is to elucidate the mechanism of assembly of this unique catalytic RNP complex and thereby understand how an RNA-binding protein influences the structure and function of its RNA ligand. 2. Use of plant RNase P to inhibit gene expression Recently, it has been demonstrated that endogenous, cellular RNase P can be guided to specifically destroy a target mRNA in bacterial and human cells in tissue culture. Our aim is to determine if plant RNase P could be utilized to disrupt gene expression in plants and their pathogens. These studies will help establish plant RNase P as a valuable functional genomics tool. Towards this objective, we have recently made significant progress in partially purifying and characterizing plant RNase P.