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Aminoacyl-tRNA synthetases

Aminoacyl-tRNA synthetases (ARS) are ubiquitous enzymes catalyzing tRNA charging by amino acids. Aminoacylated tRNAs are subsequently incorporated into proteins during translation of mRNAs on the ribosome. The team has historically worked on aminoacyl-tRNA synthetases and their tRNA substrates. Since the partition of ARS into two classes based on mutually exclusive sets of sequence motifs, the lab has deciphered the structure and functional mechanism of aspartyl-tRNA synthetase and arginyl-tRNA synthetase from Saccharomyces cerevisiae. The lab has designed and developed a set of genetic selections intended to identify and study essential residues in tRNAs and ARS. More recently, evolutionary and functional studies have been focused on leucyl-tRNA synthetase, a naturally mischarging enzyme that compensates for the imperfect substrate recognition by an efficient proofreading mechanism.

Picture of Aspartyl ARNt-synthétase