Chaperone activity of αB-crystallin suppresses tubulin aggregation through complex formation
Chaperone activity of αB-crystallin suppresses tubulin aggregation through complex formation
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DOI：
10.1247/csf.22.539
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发表时间：
1997-10-01
影响因子：
1.5
通讯作者：
Atomi, Y
中科院分区：
文献类型：
--
作者：
Arai, H;Atomi, Y
α B-晶体蛋白是一种小的热休克蛋白，在透镜和非晶状体组织中组成型表达。它可以作为其他透镜晶状体蛋白和其他一些蛋白质的分子伴侣。它的非眼功能是未知的，虽然一些报道，其中之一是有关的细胞骨架网络和/或组件。在本研究中，我们证明了α B-晶体蛋白与微管蛋白的关联。使用L 6成肌细胞裂解物与抗α B-晶体蛋白抗体的免疫沉淀实验导致α-微管蛋白的共沉淀，这显然是温度依赖性的。此外，纯化的α B-晶状体蛋白在体外37 ° C下防止纯化的微管蛋白分子的浑浊发展。蔗糖梯度离心显示，这种分子伴侣活性伴随着α B-晶体蛋白和微管蛋白二聚体的大复合物的形成。这些结果表明，α B-晶体蛋白的非透镜状功能之一可能是微管的微管蛋白亚基的保护。
alpha B-Crystallin, one of the small heat shock proteins, is constitutively expressed in lens as well as in nonlenticular tissues. It can function as a molecular chaperone for other lens crystallins and some other proteins. Its nonocular function is unknown although some reported one of them is related to cytoskeletal networks and/or components. In the present study, we demonstrate the association of alpha B-crystallin with tubulin. Immunoprecipitation experiments using L6 myoblast cell lysate with anti-alpha B-crystallin antibody resulted in the coprecipitation of alpha-tubulin, which was apparently temperature-dependent. Further, purified alpha B-crystallin prevented the turbidity development of purified tubulin molecule at 37 degrees C in vitro. Sucrose gradient centrifugation revealed that this chaperone activity was accompanied by the formation of large complex of alpha B-crystallin and tubulin dimer. These results indicate that one of the nonlenticular functions of alpha B-crystallin may be the protection of tubulin subunits of microtubules.