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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 氨基酰基TRNA合酶催化氨基酸与同源性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。出乎意料的是，细胞可以将这些管家机械驱动到超出翻译的关键信号转导途径中的新功能。例如，在肥大细胞中免疫激活后，哺乳动物赖氨酸-TRNA合成酶（LYSR）被磷酸化并转移到细胞核上。它与转录因子MITF结合，导致MITF依赖性基因表达的激活。这些新型功能需要构象切换，以将合成酶从翻译转变为信号转导。尚不清楚这种变化的细节。在这里，我们旨在收集SSRL不同状态下人类AARS的晶体衍射数据。