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RNase P catalyzes the maturation of the 5’ end of tRNA precursors. Typically these enzymes are ribonucleoproteins (RNPs) with a conserved RNA component responsible for catalysis. However, protein-only RNase P (PRORP) enzymes process precursor tRNAs in human mitochondria and all tRNA-encoded compartments of plants. PRORP enzymes represent a new class of enzymes that are conserved in all higher eukaryotes. Our work focuses on understanding how this novel class of RNase P enzymes functions by using techniques such as: steady-state and transient kinetics, mutagenesis, x-ray crystallography, crosslinking, and chemical probing of RNA. The goals of this work are to provide insights into the catalytic strategies utilized by RNA and protein that catalyze the same reaction, to gain insight into RNA maturation in mitochondria, and to understand how disease-related mutations in human mitochondrial tRNA affect RNase P processing.
Collaborators on this project:
Markos Koutmos |
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Fierke Research Group