Cyclophilin-40: evidence for a dimeric complex with hsp90.
Cyclophilin-40: evidence for a dimeric complex with hsp90.
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DOI：
10.1042/bj3070005
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发表时间：
1995-04
期刊：
影响因子：
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通讯作者：
K. Hoffmann;R. Handschumacher
中科院分区：
文献类型：
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作者：
K. Hoffmann;R. Handschumacher
人亲环素40（CyP-40）作为谷胱甘肽S-转移酶融合蛋白的表达提供了鉴定与这种普遍存在的蛋白质相关的细胞组分的手段。当融合蛋白被耦合到GSH亲和矩阵，热休克蛋白90（HSP 90）被发现是主要的相关蛋白在所有组织提取物检查。这些蛋白质中的每一种在各种组织中的相对高浓度表明，二聚体复合物以超过每一种蛋白质是其组分的无活性类固醇受体的浓度存在。协会不发生与热休克蛋白70和不受环孢菌素A（CsA）。CyP-40的两个结构域的独立表达允许N-末端异构酶和CsA结合活性从位于FKBP-59样C-末端区域的hsp 90结合位点解离。CyP-40与热休克蛋白90在许多组织中的生物学关联可能反映了蛋白质折叠和运输中的联合作用。
The expression of human cyclophilin 40 (CyP-40) as a glutathione S-transferase fusion protein has provided a means to identify cellular components that are in association with this ubiquitous protein. When the fusion protein was coupled to a GSH affinity matrix, heat-shock protein 90 (hsp90) was found to be the predominant associated protein in all tissue extracts examined. The relatively high concentration of each of these proteins in various tissues indicates that the dimeric complex exists in concentrations that exceed those of the inactive steroid receptors of which each protein is a component. Association does not occur with heat-shock protein 70 and is not affected by cyclosporin A (CsA). Independent expression of two domains of CyP-40 permitted dissociation of N-terminal isomerase and CsA binding activity from the hsp90 binding site, which is located at the FKBP-59-like C-terminal region. The biological association of CyP-40 with hsp90 in many tissues may reflect a conjoint role in protein folding and trafficking.