Poster abstracts

Poster number 13 submitted by Yiren Xu

NMR Studies of protein interactions in Archaeal RNase P

Yiren Xu (Biochemistry), Carlos Amero (Biophysics), William Boomershine (Biochemistry)

Abstract:
RNase P is an essential and ubiquitous ribonucleoprotein complex, primarily responsible for cleaving the 5’ leader sequence of precursor tRNA during their maturation. Though possessing the same function, the compositions of RNase P from three domains of life are different. Baterial RNase P has one catalytic RNA and a small protein. In archaea and eukaryotes, the enzyme is composed of one RNA and varying number of proteins. It has been demonstrated in all domains of life that it is RNA moiety that performs the catalysis, which makes RNase P a true ribozyme. However, the protein subunits are absolutely required for function of the enzyme in vivo. There are four proteins associated with the RNA in Pyrococcus furiosus RNase P, named after their human counterparts, Rpp21, Rpp29, Rpp30 and Pop5.

Previously, reconstitution assays have indicated that the four proteins work in pairs, specially: Rpp21 + Rpp29 and Rpp30 + Pop5. This project aims to elucidate the nature of the interaction between Rpp21 and Rpp29, which is the only unkown protein/protein complex structure in archaeal RNase P. By using NMR spectroscopy, we have solved the solution structure of Rpp21-Rpp29 complex. This will further provide us valuable information for the development of a 3D model the RNase P holoenzyme and improve our understanding of human RNase P.

Keywords: RNase P, archaebacteria, protein-protein interactions