2006 Ohio Student Research Forum
Abstract
Characterizing Interactions Between Ribonuclease P Subunits in ArcheaFransheska Rivera-Vega
Ohio State University (University of Puerto Rico-Mayaguez)
Department of Industrial Biotechnology
Mentor: Dr. Mark P. Foster, Yiren Xu
Ribonuclease P (RNase P) is a ribonucleoprotein complex present in all domains of life. This essential enzyme is involved in the maturation of precursor-tRNA molecules. The maturation step catalyzed by RNase P involves cleaving the 5’ end of precursor tRNA molecules and is required for tRNA function. RNase P is comprised of one RNA subunit and proteins whose number and identity vary by domain of life. Archaeal RNase P is comprised of an RNA subunit plus four protein subunits. In the thermophilic archaeon, Metanothermobacter thermoautotrophicus (Mth), each of its four proteins, Rpp21, Rpp29, Rpp30 and Pop5, is homologous to a protein subunit in the human enzyme. Because the archaeal proteins are smaller and better suited to biophysical characterization, Mth RNase P is being studied as a model to understand the complexity of the RNase P in humans and other eukaryotes.
In this study, we are using NMR spectroscopy to study the interaction between two Mth proteins: Rpp21 and Rpp29. These studies will help to describe and characterize the proteins subunits that form RNase P, and eventually reveal the structure of the entire enzyme. Understanding the organization and function of RNase P in archaeal organisms will provide a good foundation for understanding the function of human RNase P.
The approach taken and some results of the study will be presented.
