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

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。氨基酰基trna合成酶是一个负责将氨基酸与同源trna结合的酶家族。有趣的是，酵母线粒体LeuRS不仅参与氨基酸酰化，还参与酵母线粒体I族内含子的RNA剪接。我们发现酵母线粒体LeuRS的c端改变会影响其剪接活性。然而，当LeuRS的整个c端结构域被删除时，其氨基酰化和氨基酸编辑活性增强。因此，我们想要确定野生型和c端缺失突变体的leucyl-tRNA合成酶的结构和折叠完整性。

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.