2 MAMMALIAN HEAT-SHOCK PROTEINS, HSP90 AND HSP100, ARE ACTIN-BINDING PROTEINS
2 MAMMALIAN HEAT-SHOCK PROTEINS, HSP90 AND HSP100, ARE ACTIN-BINDING PROTEINS
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DOI：
10.1073/pnas.83.21.8054
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发表时间：
1986-11-01
影响因子：
11.1
通讯作者：
YAHARA, I
中科院分区：
文献类型：
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作者：
KOYASU, S;NISHIDA, E;YAHARA, I
分别从小鼠淋巴瘤细胞系L5178Y培养细胞的提取物中纯化出两种高分子量热休克蛋白HSP90 （Mr, 90,000）和HSP100 （Mr, 100,000）。两种热休克蛋白在生理条件下均以二聚体形式存在。它们的物理化学性质非常相似。在肌动蛋白聚合条件下，每一种纯化的热敏感蛋白都能与兔骨骼肌肌动蛋白共沉淀。HSP90和HSP100都以剂量依赖性的方式增加了丝状肌动蛋白溶液的低剪切粘度，这表明这些HSP90和HSP100可以交联肌动蛋白丝。虽然HSP90和HSP100在肌动蛋白溶液中的一些分子性质和上述作用与α相似。- actitin， HSPs与。alpha区分开来。-肌动蛋白通过各种手段，包括在低角度旋转阴影技术的帮助下通过电子显微镜观察分子形状。HSP90特异性抗血清免疫荧光染色显示，HSP90除局限于细胞质间隙外，还局限于皱膜。
Two high molecular weight heat shock proteins, HSP90 (Mr, 90,000) and HSP100 (Mr, 100,000), were separately purified from extracts of cultured cells of a mouse lymphoma cell line, L5178Y. Both of the HSPs exist in homodimeric form under physiological conditions. Their physicochemical properties are quite similar to each other. Each of the purified HSPs was shown to coprecipitate with rabbit skeletal muscle actin under actin-polymerizing conditions. Both HSP90 and HSP100 increased the low-shear viscosity of filamentous actin solutions in a dose-dependent manner, which suggests that these HSPs cross-link actin filaments. Although some molecular properties and the effects described above on actin solution of HSP90 and HSP100 resemble those of .alpha.-actinin, the HSPs were distinguished from .alpha.-actinin by various means, including visualization of molecular shapes by electron microscopy with the aid of the low-angle rotary shadowing technique. Immunofluorescence staining by specific antisera against HSP90 revealed that HSP90 was localized in ruffling membranes in addition to the cytoplasmic space.