CRYSTAL STRUCTURE OF AMINOACYL-TRNA SYNTHETASES AT MULTI-FUNCTIONAL STATES

多功能状态下氨基酰基-TRNA 合成酶的晶体结构

• 批准号: 8362430
• 负责人: Min Guo
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362430
• 关键词: Algorithms; Amino Acids; Amino Acyl-tRNA Synthetases; Binding; Cell Nucleus; Cells; Funding; Gene Expression; Genetic Code; Grant; Housekeeping; Ligase; Lysine-tRNA Ligase; National Center for Research Resources; Principal Investigator; Protein Biosynthesis; Radiation; Reaction; Research; Research Infrastructure; Resources; Signal Transduction; Signal Transduction Pathway; Source; Structure; Transfer RNA; Translations; United States National Institutes of Health; cost; human data; immune activation; mast cell; novel; structural biology; transcription factor

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Aminoacyl tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs. They establish the algorithm of the genetic code in this first reaction of protein synthesis. Surprisingly, cells can drive these housekeeping machineries into novel functions in key signal transduction pathways beyond translation. For example, upon immune activation in mast cells, mammalian lysyl-tRNA synthetase (LysRS) is phosphorylated and translocated to the nucleus. It binds to transcription factor MITF, leading to the activation of MITF-dependent gene expression. These novel functions require conformational switch to redirect the synthetases from translation to signal transduction. Not known are the particulars of such changes. Here we aim to collect crystal diffraction data of the human aaRSs at different states at SSRL.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 氨酰 tRNA 合成酶催化氨基酸与其同源 tRNA 的附着。他们在蛋白质合成的第一个反应中建立了遗传密码的算法。令人惊讶的是，细胞可以驱动这些管家机器在翻译之外的关键信号转导途径中发挥新功能。例如，肥大细胞中的免疫激活后，哺乳动物赖氨酰-tRNA 合成酶 (LysRS) 被磷酸化并易位至细胞核。它与转录因子 MITF 结合，导致 MITF 依赖性基因表达的激活。这些新功能需要构象转换来将合成酶从翻译重定向到信号转导。这些变化的具体细节尚不清楚。在这里，我们的目标是在 SSRL 收集人类 aaRS 在不同状态下的晶体衍射数据。