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哺乳动物微管相关蛋白2(MAP2)与烟草微管蛋白共聚过程中的成核缺陷。

Deficient nucleation during co-polymerization of mammalian MAP2 and tobacco tubulin.

作者信息

Hugdahl J D, Morejohn L C

机构信息

Department of Botany, University of Texas at Austin 78713.

出版信息

Biochem Mol Biol Int. 1994 Sep;34(2):375-84.

PMID:7849649
Abstract

To obtain information on the functional domains of tubulin from a dicot plant, we investigated the interactions of tobacco tubulin with MAP2 from bovine brain supernatant. Taxol-stabilized tobacco and bovine brain microtubules had similar binding capacities for MAP2 (1 mol MAP2 per 8-9 mol tubulin). However, MAP2 dissociated from tobacco microtubules more readily than from bovine brain microtubules and induced the polymerization of tobacco tubulin into aberrant helical ribbon polymers, rather than microtubules. Ribbon assembly was partially suppressed by 50 mM KCl. Abundant tobacco microtubules formed when MAP2-induced nucleation was by-passed with microtubule seeds. Thus, deficient nucleation of tobacco tubulin assembly by MAP2 reflects distinct properties of the polymerization and regulatory domains of plant and animal tubulins.

摘要

为了获取双子叶植物微管蛋白功能结构域的信息,我们研究了烟草微管蛋白与牛脑上清液中微管相关蛋白2(MAP2)的相互作用。紫杉醇稳定的烟草微管和牛脑微管对MAP2具有相似的结合能力(每8 - 9摩尔微管蛋白结合1摩尔MAP2)。然而,MAP2从烟草微管上解离比从牛脑微管上更容易,并且诱导烟草微管蛋白聚合成异常的螺旋带状聚合物,而不是微管。50 mM KCl可部分抑制带状聚合物的组装。当用微管种子绕过MAP2诱导的成核作用时,会形成大量的烟草微管。因此,MAP2诱导烟草微管蛋白组装时成核作用不足,反映了植物和动物微管蛋白在聚合和调节结构域上的不同特性。

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