酵母γ-微管蛋白复合体的Spc98p和Spc97p通过与Spc110p相互作用介导与纺锤体极体的结合。
Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p.
作者信息
Knop M, Schiebel E
机构信息
Max-Planck Institut für Biochemie, Genzentrum, Am Klopferspitz 18a, 82152 Martinsried, Germany.
出版信息
EMBO J. 1997 Dec 1;16(23):6985-95. doi: 10.1093/emboj/16.23.6985.
Previously, we have shown that the yeast gamma-tubulin, Tub4p, forms a 6S complex with the spindle pole body components Spc98p and Spc97p. In this paper we report the purification of the Tub4p complex. It contained one molecule of Spc98p and Spc97p, and two or more molecules of Tub4p, but no other protein. We addressed how the Tub4p complex binds to the yeast microtubule organizing center, the spindle pole body (SPB). Genetic and biochemical data indicate that Spc98p and Spc97p of the Tub4p complex bind to the N-terminal domain of the SPB component Spc110p. Finally, we isolated a complex containing Spc110p, Spc42p, calmodulin and a 35 kDa protein, suggesting that these four proteins interact in the SPB. We discuss in a model, how the N-terminus of Spc110p anchors the Tub4p complex to the SPB and how Spc110p itself is embedded in the SPB.
此前，我们已经表明，酵母γ-微管蛋白Tub4p与纺锤体极体组分Spc98p和Spc97p形成一个6S复合物。在本文中，我们报道了Tub4p复合物的纯化。它包含一个Spc98p分子和Spc97p分子，以及两个或更多个Tub4p分子，但不含其他蛋白质。我们探讨了Tub4p复合物如何与酵母微管组织中心即纺锤体极体（SPB）结合。遗传和生化数据表明，Tub4p复合物的Spc98p和Spc97p与SPB组分Spc110p的N端结构域结合。最后，我们分离出了一个包含Spc110p、Spc42p、钙调蛋白和一种35 kDa蛋白质的复合物，这表明这四种蛋白质在SPB中相互作用。我们在一个模型中讨论了Spc110p的N端如何将Tub4p复合物锚定到SPB上，以及Spc110p本身如何嵌入SPB中。
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