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

亮氨酰-TRNA 合成酶独特 C 端结构域的功能差异

• 批准号: 7357995
• 负责人: SUSAN A MARTINIS
• 金额: $ 0.69万
• 依托单位: UNIVERSITY OF CALIFORNIA-IRVINE
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-08-29 至 2007-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7357995
• 关键词: RNA splicing; aminoacid tRNA ligase; enzymes; family; introns; mitochondria; mutant; yeasts

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.

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。氨基酰-tRNA合成酶是一个酶家族，负责将氨基酸充电到其同源tRNA上。有趣的是，酵母线粒体LEUS不仅参与氨基酰化，而且还参与酵母线粒体内含子I的RNA剪接。我们发现酵母线粒体轻链C末端的改变会影响其剪接活性。然而，当LEUR的整个C-末端结构域被删除时，其氨基酰化和氨基酸编辑活性增强。因此，我们想要确定亮氨酰-tRNA合成酶野生型和C端缺失突变体的结构和折叠完整性。