Friday, October 8, 2010
RNS 390 at 3:15 p.m. with refreshments served prior to seminar.
Associate Professor of Chemistry
Director of Carleton's Interdisciplinary Science and Math Initiative
Director of Biochemistry
Piecing together a molecular puzzle -
mitochondrial alanyl-tRNA synthetases
The aminoacyl-tRNA synthetases the keepers of the genetic code - each of these enzymes must catalyze the attachment of a specific amino acid to the set of transfer RNAs that bear the corresponding anticodon, ensuring that DNA codons are correctly translated into proteins. Animal cells have a distinct set of tRNAs in the cytoplasm and another in the mitochondria, so in many cases they require two aminoacyl-tRNA synthetases for each amino acid. The mitochondrial enzymes can differ considerably in structure and function from their cytoplasmic counterparts, and relatively little is known about them.
Work in my lab has focused on characterizing the molecular
interactions between mitochondrial alanyl-tRNA synthetases and their RNA substrates. Understanding these oddballs has provided interesting insights about the evolution of RNA recognition in general and the mode of action of alanyl-tRNA synthetases in particular.