SOLUTION STRUCTURE OF THE SIGNAL RECOGNITION PARTICLE FROM T AQUATICUS: A SAXS

T AQUATICUS 信号识别粒子的解决方案结构：SAXS

• 批准号: 7598025
• 负责人: Robert M Stroud
• 金额: $ 0.3万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598025
• 关键词: Binding; Cell membrane; Charge; Complex; Computer Retrieval of Information on Scientific Projects Database; Endoplasmic Reticulum; Eubacterium; Funding; GTPase-Activating Proteins; Gel Chromatography; Grant; Guanosine Triphosphate; Guanosine Triphosphate Phosphohydrolases; Hydrolysis; Institution; Life; Membrane; Membrane Proteins; Modeling; Molecular; Molecular Conformation; Nucleotides; Pathway interactions; Peptide Signal Sequences; Protein Overexpression; Protein translocation; Proteins; RNA; Research; Research Personnel; Resolution; Resources; Ribosomes; Shapes; Signal Recognition Particle; Solutions; Source; Structure; Techniques; Thermus; Translating; United States National Institutes of Health; analytical ultracentrifugation; light scattering; receptor

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. The signal recognition particle (SRP) and its membrane-associated receptor (SR) constitute an evolutionary conserved macromolecular ribonucleoproteic complex that catalyzes targeting of nascent secretory and membrane proteins to the protein translocation apparatus. The SRP is in charge of directing ribosomes which are currently translating proteins destined for either secretion or membrane integration to the endoplasmic reticulum or plasma membrane. The receptor is responsible for the targeting of the ribosome-nascent protein-SRP complex to the membrane translocation machinery. The components of the SRP pathway and the essential steps of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life. The thermostable signal recognition particle from the eubacteria Thermus aquaticus (Taq) is a ribonucleic acid-protein complex composed of the SRP-RNA, which is 113 nucleotides long (35 kDa), and two proteins, the receptor subunit FtsY (33 kDal) and the RNA and signal sequence-binding subunit Ffh (48 kDa). In addition both proteins are structurally related GTPases and GTP-dependent GTPase-activating proteins (GAPs). The ribosome-nascent protein-SRP complex interaction with its receptor is also GTP dependent. GTP hydrolysis by the SRP-SR complex dissociates this complex, allowing a new round of targeting. All components of the Taq-SRP are overexpressed and soluble and have been extensively characterized by gel filtration, dynamic light scattering and analytical ultracentrifugation, in terms of homogeneity and stability. The aim of this biophysical study by SAXS is to charactize the shapes and the conformations of the Taq-SRP and its subcomponents in solution. Since the crystal structures of the isolated subunits are available, using SAXS techniques we wish to construct low-resolution models of the binary (FtsY/Ffh) and ternary (FtsY/Ffh/SRP-RNA) complexes whose structures are still unknown.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 信号识别颗粒（SRP）及其与膜相关的受体（SR）构成了一种进化保守的大分子核糖核蛋白蛋白蛋白蛋白蛋白蛋白蛋白质复合物，该复合物将靶向新生的分泌和膜蛋白促进蛋白质易位。 SRP负责指导核糖体，这些核糖体目前正在将原定为分泌或膜整合到内质网或质膜整合的蛋白质。 该受体负责将核糖体 - 含量蛋白-SRP复合物靶向膜易位机械。 SRP途径的成分和SRP依赖性蛋白靶向的分子机理的基本步骤在生命的所有三个王国中都保守。来自Eubacteria Thermus aquaticus（TAQ）的热稳定信号识别颗粒是由SRP-RNA组成的核糖核酸 - 蛋白质复合物，该复合物由SRP-RNA组成，SRP-RNA是113个核苷酸长（35 kDa），两个蛋白质，受体亚基FTSY FTSY（33 kDal）和rNA和信号序列序列序列序列序列构成（48）（48）另外，两种蛋白质都是与结构相关的GTPases和GTP依赖性GTPase激活蛋白（GAPS）。核糖体 - 脱粒蛋白-SRP复合物与其受体的相互作用也依赖于GTP。 SRP-SR复合物的GTP水解解离了该复合物，从而允许新的靶向靶向。 TAQ-SRP的所有组件都过表达和可溶性，并且在同质性和稳定性方面，以凝胶过滤，动态光散射和分析性超速离心为特征。 SAXS的这项生物物理研究的目的是使Taq-SRP及其在溶液中的亚组成部分的形状和构象归纳。由于可以使用隔离亚基的晶体结构，因此我们希望使用SAXS技术构建二元（FTSY/FFH）的低分辨率模型和三元（FTSY/FFH/SRP-RNA）络合物，其结构仍然未知。