CHED 854 |
| Metazoan mitochondria contain tRNAs which are highly diverged in both sequence and structure from those found elsewhere in evolution. These tRNAs are recognized and specifically charged by nuclearly encoded mitochondrial aminoacyl-tRNA synthetases. Our work is focused on characterizing the interaction between human mitochondrial alanyl-tRNA synthetase (Hs mt AlaRS) and its tRNA substrate. Mutational analysis of both the enzyme and tRNA substrate estabilished that contacts between the acceptor stem and the N-terminal domains of the enzyme are relatively unimportant for establishing tRNA identity, in contrast to all previously characterized alanyl-tRNA synthetases. However, the C-terminal half of Hs mt AlaRS and the D-acceptor domain of the tRNA are required for aminoacylation, suggesting that in the human mitochondrial system a second set of tRNA-AlaRS contacts plays a role in determining tRNAAla identity. Because mitochondrial tRNAs are structurally fragile, we have used in-line probing to validate RNA secondary and tertiary structure. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |