American Society for Microbiology, National Meeting (1998), Atlanta, GA.

The Catalytic Activity of Archaeal RNase P RNA

James Pannucci*, Elizabeth S. Haas and James W. Brown
Dept. of Microbiology, North Carolina State Univ. Raleigh, NC.

RNase P is an endoribonuclease that contains both an RNA and a protein subunit. It the enzyme responsible for the maturation of the 5' end of precursor tRNA molecules. The bacterial RNase P RNA is catalytically active in vitro without its protein subunit, but that characteristic has not been reproducibly demonstrated in similar tests by an RNase P RNA from the Archaea. Comparisons of RNase P RNAs from the bacterial and archaeal evolutionary domains show a high degree of structural similarity, but the differences that are present may be responsible for altering in vitro catalytic ability. The following research examines the catalytic activity of archaeal RNase P RNAs by establishing assay conditions that promote in vitro catalysis. Determining these requirements should resolve why archaeal RNase P RNAs were thought to be inactive in vitro and further the understanding of the relationship between structure and function in catalytic RNAs.