The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain.
The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain.
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亲免蛋白 FKBP59-HBI 与 90-kDa 热休克蛋白相互作用的能力由其四三肽重复结构域编码。
DOI：
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发表时间：
1994
影响因子：
11.1
通讯作者：
E. Baulieu
中科院分区：
文献类型：
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作者：
C. Radanyi;B. Chambraud;E. Baulieu
fk506结合蛋白类（FKBP59）的表观分子质量约为59 kDa，与非转化类固醇受体复合物中的热休克蛋白hsp90相关，称为FKBP59-HBI （HBI为热休克蛋白90 Binding Immunophilin）。进一步的数据分析表明，该亲免疫蛋白也属于四肽重复蛋白家族。在这项工作中，我们描述了FKBP59-HBI的hsp90结合域。密度梯度离心、凝胶过滤和免疫吸附分析均未能证明兔网织细胞裂解液中FKBP59-HBI与hsp90之间存在稳定的关联。通过凝胶阻滞实验，我们提供了高纯度野生型兔FKBP59-HBI与人hsp90 β之间特异性atp不依赖相互作用的证据。这种相互作用不受免疫抑制剂FK506和雷帕霉素的影响。对几个突变体的行为检查使我们得出结论，定位在FKBP59-HBI的c端部分的四肽基序是hsp90结合所必需的。
A protein of apparent molecular mass of approximately 59 kDa of the FK506-binding protein class (FKBP59) has been found associated with the heat shock protein hsp90 included in nontransformed steroid receptor complexes and termed FKBP59-HBI (HBI for Heat shock protein 90 Binding Immunophilin). Further data analysis has revealed that this immunophilin also belongs to the tetratricopeptide repeat family of proteins. In this work, we describe the hsp90-binding domain of FKBP59-HBI. Density gradient centrifugation, gel filtration, and immunoadsorption analyses failed to demonstrate a stable association between FKBP59-HBI and hsp90 in the rabbit reticulocyte lysate. Using a gel-retardation assay, we provide evidence for a specific ATP-independent interaction between highly purified wild-type rabbit FKBP59-HBI and human hsp90 beta. This interaction was not affected by the immunosuppressants FK506 and rapamycin. Examination of the behavior of several mutants led us to conclude that the tetratricopeptide motifs localized in the C-terminal part of FKBP59-HBI are necessary for hsp90 binding.