RNA 的时间恢复羟基自由基足迹-猫眼课题宝

RNA 的时间恢复羟基自由基足迹

批准号：

7317750

负责人：

SARAH A. WOODSON

金额：

$32.21万

依托单位：

JOHNS HOPKINS UNIVERSITY

依托单位国家：

美国

项目类别：

财政年份：

1999

资助国家：

美国

项目状态：

已结题

起止时间：

1999-05-01 至 2011-07-31

来源：

https://reporter.nih.gov/project-details/7317750

关键词：

Address Anti-Bacterial Agents Antiviral Agents Azoarcus Binding Binding Proteins Binding Sites Biochemical Biogenesis Biological Assay Biological Models Catalytic RNA Cells Complex Dependence Digestion Disease Drug Delivery Systems Ensure Escherichia coli Fluorescence Fluorescence Resonance Energy Transfer Fragile X Syndrome Gel Genes Goals Helix (Snails)Hereditary Disease Human Hydroxyl Radical In Situ In Vitro Individual Kinetics Label Lead Link Measures Mental Retardation Methods Monitor Muscular Dystrophies Mutation Normal Cell Organism Pathway interactions Phenotype Process Protein Binding Proteins Quality Control RNA RNA Binding RNA Folding RNA Recognition Motif RNA Stability RNA-Protein Interaction Research Ribonucleases Ribosomal Proteins Ribosomal RNA Ribosomes Roentgen Rays Role Shapes Site Site-Directed Mutagenesis Son of Sevenless Proteins Structure Testing Time Translating Vertebral column base cell growth design ear helix gel mobility shift assay group I ribozyme insight protein structure rRNA Precursor stopped-flow fluorescence thermostability three dimensional structure time use tumor

项目摘要

项目成果

SARAH A. WOODSON的其他基金

相似基金

相关文献

中文摘要

翻译

点击翻译按钮获取中文摘要

英文摘要

DESCRIPTION (provided by applicant): In all organisms, RNA molecules are needed to translate genes into protein, and to turn specific genes on and off. The malfunction of controlling RNAs has been linked to diseases such as muscular dystrophy, Fragile X mental retardation, and certain tumors. In order to function normally, RNAs must fold into specific three-dimensional shapes and must assemble with particular proteins. For example, the ribosome contains two large RNAs and more than 50 proteins which must come together in precisely the right way. The goal of this research is to understand how RNAs fold up, and how they cooperate with proteins to form cellular "machines" such as the ribosome. The results will help understand how certain RNAs malfunction in human, genetic diseases, and will assist the design of antibacterial and antiviral drugs. We have previously used time-resolved hydroxyl radical footprinting, small angle scattering and biochemical methods to probe the folding pathway of ribozymes. Recently, we have used footprinting to follow the assembly of the SOS ribosome in real time. In the first aim, a stable bacterial group I ribozyme will be used as a model system to dissect the interactions that cooperatively stabilize RNA tertiary structure. The principles of RNA folding obtained from studies of ribozymes will be applied to assembly of SOS ribosomes in aims 2-4. The formation of RNA and RNA-protein interactions will be monitored by protection of the RNA backbone from hydroxyl radical cleavage and by changes in the fluorescence of labeled RNAs. Questions to be addressed are (1) how proteins recognize their binding sites and stabilize tertiary interactions in the rRNA, (2) whether proteins change the ribosomal RNA folding pathway, and (3) folding and assembly of the pre-168 rRNA. Long-term goals are to establish assays for ribosome assembly in situ, and to understand the link between the fidelity of RNA folding, assembly and processing of the pre-rRNA.

期刊论文(0)

专著(0)

科研奖励(0)

会议论文