REFINING THE STRUCTURE OF THE SMALL GAMMA TUBULIN COMPLEX

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 小的伽马微管蛋白复合体是微管成核单位的一部分。该络合物由两个Tub4P和一个 Spc97p和Spc98p中的每一个。Tub4p，伽马微管蛋白，结合α-β微管蛋白异源二聚体，构建 微管。双杂交实验表明，Spc110与Spc98和Spc97相互作用，与Tub4相互作用较弱。 Spc110能够在杆状病毒提取物的IP实验中直接结合Spc98。Spc110提供了在 通过与Spc97和Spc98相互作用，形成微管蛋白复合体和纺锤体极体(Spb)的内部斑块。 我们的目标是在体内使用FRET来完善Tub4p复合体的结构。

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 baculovirus 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.