TUB4 COMPLEX IN YEAST

酵母中的 TUB4 复合物

• 批准号: 8171267
• 负责人: Trisha N. Davis
• 金额: $ 0.24万
• 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/8171267
• 关键词: Baculoviruses; Centrosome; Collaborations; Complex; Computer Retrieval of Information on Scientific Projects Database; Eukaryotic Cell; Funding; Grant; Institution; Microtubules; Nuclear; Organelles; Proteins; Research; Research Personnel; Resources; Source; United States National Institutes of Health; Work; Yeasts; gamma Tubulin; reconstitution; spindle pole body

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 yeast spindle pole body (SPB) is functionally equivalent to the centrosome in higher eukaryotic cells. The SPB is a multilayered organelle that organizes both the nuclear and cytoplasmic microtubules. We are working toward reconstitution of the microtubule nucleating activity of the SPB. The well characterized small gamma-tubulin complex contains three proteins: Tub4p, Spc97p, and Spc98p. We have expressed all three proteins in baculovirus and found that they readily assemble into a stable, soluble complex. However, the nucleation capacity of the small complex is quite low, suggesting we are missing components required for nucleation. The yeast spindle pole body (SPB) is functionally equivalent to the centrosome in higher eukaryotic cells. The SPB is a multilayered organelle that organizes both the nuclear and cytoplasmic microtubules. We are working toward reconstitution of the microtubule nucleating activity of the SPB. The well characterized small gamma-tubulin complex contains three proteins: Tub4p, Spc97p, and Spc98p. We have expressed all three proteins in baculovirus and found that they readily assemble into a stable, soluble complex. However, the nucleation capacity of the small complex is quite low. Recently the Agard lab (in collaboration with us) showed that the Tub4p molecules in the small complex are too far apart to nucleate microtubules.

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。 酵母纺锤体体（SPB）在功能上等同于较高的真核细胞中的中心体。 SPB是一种多层细胞器，可组织核和细胞质微管。 我们正在努力重建SPB的微管成核活性。 特征良好的小γ-微管蛋白复合物包含三种蛋白质：TUB4P，SPC97P和SPC98P。我们已经在杆状病毒中表达了所有三种蛋白质，发现它们很容易组装成稳定的可溶性复合物。但是，小复合物的成核能力很低，这表明我们缺少成核所需的组件。酵母纺锤体体（SPB）在功能上等同于较高的真核细胞中的中心体。 SPB是一种多层细胞器，可组织核和细胞质微管。 我们正在努力重建SPB的微管成核活性。 特征良好的小γ-微管蛋白复合物包含三种蛋白质：TUB4P，SPC97P和SPC98P。我们已经在杆状病毒中表达了所有三种蛋白质，发现它们很容易组装成稳定的可溶性复合物。但是，小复合物的成核能力很低。 最近，Agard Lab（与我们合作）表明，小型复合物中的TUB4P分子相距太远，无法将微管核定。