Two separate 18-amino acid domains of tau promote the polymerization of tubulin.

Two separate 18-amino acid domains of tau promote the polymerization of tubulin.
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DOI:
10.1016/s0021-9258(18)83547-5
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发表时间:
1989-04
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
D J Ennulat;R K Liem;G A Hashim;M. L. Shelanski
D J Ennulat;R K Liem;G A Hashim;M. L. Shelanski
中科院分区:
其他
文献类型:
--
作者:
D J Ennulat;R K Liem;G A Hashim;M. L. Shelanski

文献摘要

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Tau 是一种热稳定的微管相关蛋白,可促进微管蛋白聚合。使用以人类和小鼠 tau 中发现的结构域为模型的合成肽来定位 tau 的组装促进区域。这些合成肽的设计基于小鼠 tau 蛋白中发现的三重重复基序。第一个肽 Tau-(187–204) 和第二个肽 Tau-(218–235) 在浓度高于 100 µM 时能够促进微管蛋白聚合成微管。测试的另外两种肽 TauR 和 Tau-(250–267) 在高达 800 µM 的浓度范围内无法促进微管蛋白的组装。 TauRi 是 Tau-(187–204) 的随机类似物。尽管 TauRis 无法促进聚合,但它可以修饰 Tau-(187-204) 诱导的微管蛋白组装。
Tau is a heat-stable microtubule-associated protein which promotes tubulin polymerization. The assembly promoting region of tau was localized using synthetic peptides modeled after domains found in both human and mouse tau. The design of these synthetic peptides was based on the triple repeat motif found in mouse tau. The first peptide, Tau-(187–204), and the second peptide, Tau-(218–235), are capable of promoting the polymerization of tubulin into microtubules, at concentrations above 100 µM. Two other peptides tested, TauRand Tau-(250–267), were not able to promote the assembly of tubulin over a range of concentrations up to 800 µM. TauRis a random analog of Tau-(187–204). Although TauRis unable to promote polymerization, it can modify Tau-(187–204)-induced tubulin assembly.