Yeast Mitochondrial Threonyl-tRNA Synthetase (MST1) as a Model Enzyme for Studying High Fidelity Information: a Multi-scale Computational Chemistry Study
In order for the body to function properly, information from DNA must be translated correctly into proteins. One group of enzymes critical to this process is the aminoacyl-tRNA synthetases (aaRS). These enzymes attach an amino acid to its cognate tRNA, which delivers them to make proteins. Although this process is critical to the survival of the organism, the details of how the cell achieves such high fidelity and error-free task is not completely understood. Since some amino acids are so similar to each other, aaRS must be able to remove incorrectly attached amino acid-tRNA pairs. In particular, our research focuses on the mechanism of how threonyl-tRNA synthetases (ThrRS) are able to remove incorrectly paired serine-AMP pairs using computational chemistry. This is important because ThrRS have been found to be involved in ovarian cancer, autoimmune diseases, and neurodegeneration.
Understanding the ThrRS editing mechanism may lead to possible treatment for these diseases.