Dissecting Catalytic Features of Diverse Methionyl-tRNA Synthetase Enzymes

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Protein synthesis is one of the most critical cellular activities of any organism. Aminoacyl-tRNA synthetases are essential enzymes in protein biosynthesis, catalyzing the attachment of amino acids to tRNA adaptors for ribosomal decoding of genetic information. Many tRNA synthetases have additional roles in cellular regulation separate from their function in translation. This project investigates mechanistic features of methionyl-tRNA synthetase, which is a distinctive tRNA synthetase in that its tRNA isoacceptors have divergent fates in translational initiation versus elongation. The tRNA synthetases exist in both monomeric and dimeric forms in different organisms, and, in some organisms, they contain appended protein domains that expand their cellular functions. Using tools of molecular biology, computational chemistry, and mechanistic enzymology, this research seeks to expand understanding of evolutionarily distinct methionyl-tRNA synthetase enzymes in protein biosynthesis and novel cellular activities. Broader Impacts. The project provides training in modern biological chemistry techniques to emerging scientists at Wake Forest University, a liberal arts university. The local community is impacted through after-school science clubs offering hands-on enrichment activities for at-risk middle school students. These science clubs are led by undergraduate students in a seminar course on the history of women in science, thus providing a real-world example of the challenges inherent in increasing participation of populations typically underrepresented in science.