NS3 HELICASE

NS3解旋酶

• 批准号: 7953792
• 负责人: Kevin Douglas Raney
• 金额: $ 0.87万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-12-01 至 2009-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7953792
• 关键词: Boxing; Collaborations; Computer Retrieval of Information on Scientific Projects Database; DNA; DNA-Protein Interaction; Data; Electron Microscopy; Equilibrium; Filament; Funding; Grant; Hepatitis C virus; Institution; Manuscripts; Metabolism; Methods; Molecular Motors; Motor; Proteins; Publishing; RNA; RNA Sequences; RNA Viruses; RNA replication; Research; Research Personnel; Resources; Source; Structural Protein; Structure; United States National Institutes of Health; Viral; Virus Replication; experience; helicase; macromolecule

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. RNA metabolism requires the action of numerous ATP-dependent, molecular motor proteins that are believed to transport, remodel, and unwind secondary structures in RNA sequences. Many of these molecular motors are DEAD-box or closely related proteins. Many positive strand RNA viruses, such as the hepatitis C virus (HCV), require the activity of these proteins for RNA replication. Determination of the mechanism of these proteins and their specific functions is of fundamental importance to our understanding of viral replication as well as RNA metabolism in general. Non-structural protein 3 (NS3) is an RNA motor protein (or helicase), that is necessary for HCV replication. Our data supports the hypothesis that NS3 exists in equilibrium between monomeric and oligomeric species, and that its RNA unwinding activity increases with increasing oligomerization. Our data suggest that NS3 helicase can form filaments on RNA and DNA. We wish to establish a collaborative effort to visualize these filaments. The attached manuscripts describes some of our evidence for filament formation on DNA. However, most of the data supporting filament formation is yet to be published. We wish to establish this collaboration in order to thoroughly investigate protein-protien and protein-DNA interactions of NS3. We have no experience in EM, but are aware of numerous examples in which filament formation has been characterized by this method.

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。 RNA代谢需要众多依赖ATP的分子运动蛋白的作用，这些蛋白被认为可以在RNA序列中运输，重塑和未固定的二级结构。 这些分子电动机中的许多是死箱或密切相关的蛋白质。 许多阳性链RNA病毒，例如丙型肝炎病毒（HCV），都需要这些蛋白质的活性进行RNA复制。 确定这些蛋白质及其特定功能对于我们对病毒复制以及总体上RNA代谢的理解至关重要。非结构蛋白3（NS3）是一种RNA运动蛋白（或解旋酶），是HCV复制所必需的。 我们的数据支持以下假设：NS3在单体和低聚物种之间存在平衡，并且其RNA放松活性随着寡聚的增加而增加。 我们的数据表明，NS3解旋酶可以在RNA和DNA上形成丝。 我们希望建立合作的努力来可视化这些细丝。 所附的手稿描述了我们在DNA上形成细丝的一些证据。 但是，大多数支持细丝形成的数据尚未公布。 我们希望建立这种合作，以彻底研究NS3的蛋白质 - 蛋白质和蛋白-DNA相互作用。我们没有在EM上的经验，但是知道了许多示例，其中已通过这种方法表征了细丝形成。