REFINING THE STRUCTURE OF THE SMALL GAMMA TUBULIN COMPLEX

细化小伽玛微管蛋白复合物的结构

• 批准号: 8171350
• 负责人: DAVID A. AGARD
• 金额: $ 0.96万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-09-01 至 2011-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171350
• 关键词: Binding; Complex; Computer Retrieval of Information on Scientific Projects Database; Fluorescence Resonance Energy Transfer; Funding; Goals; Grant; Institution; Link; Microtubules; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; beta Tubulin; gamma Tubulin; in vivo; research study; spindle pole body; yeast two hybrid system

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 small gamma tubulin complex is part of the microtubule-nucleating unit. The complex consists of two Tub4p and one each of Spc97p and Spc98p. Tub4p, gamma tubulin, binds the alpha-beta tubulin heterodimer, the building blocks of microtubules. Two-hybrid experiments have shown that Spc110 interacts with Spc98 and Spc97 and weakly with Tub4. Spc110 is able to directly bind Spc98 in IP experiments from baclovirus extracts. Spc110 provides the link between the gamma tubulin complex and the inner plaque of the spindle pole body (SPB) through its interaction with Spc97 and Spc98. Our goal is to use FRET to refine the structure of the Tub4p complex in vivo.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 小γ微管蛋白复合物是微管成核单元的一部分。该复合物由两个Tub 4p和一个Spc 97 p和一个Spc 98 p组成。Tub 4p，γ微管蛋白，结合α-β微管蛋白异二聚体，微管的构建块。双杂交实验表明，Spc 110与Spc 98和Spc 97相互作用，与Tub 4相互作用较弱。在杆状病毒提取物的IP实验中，Spc 110能够直接结合Spc 98。Spc 110通过其与Spc 97和Spc 98的相互作用提供γ微管蛋白复合物与纺锤体极体（SPB）的内斑块之间的联系。 我们的目标是使用FRET来完善体内Tub 4p复合物的结构。