FUNCTIONAL DIVERGENCE OF A UNIQUE C-TERMINAL DOMAIN OF LEUCYL-TRNA SYNTHETASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Aminoacyl-tRNA synthetases are a family of enzymes that is responsible for charging amino acids to their cognate tRNAs. Interestingly, the yeast mitochondrial LeuRS not only participates in aminoacylation but also in RNA splicing of group I introns in the yeast mitochondria. We found that alterations at the C-terminus of yeast mitochondrial LeuRS impacted its splicing activity. However, when the entire C-terminal domain of the LeuRS was deleted, its aminoacylation and amino acid editing activities were enhanced. As a result, we would like to determine the structural and folding integrity of the wild-type and the C-terminal deletion mutant of leucyl-tRNA synthetase.