Chambraud B, Rouvière-Fourmy N, Radanyi C, Hsiao K, Peattie D A, Livingston D J, Baulieu E E
INSERM U33, Kremlin Bicêtre, France.
Biochem Biophys Res Commun. 1993 Oct 15;196(1):160-6. doi: 10.1006/bbrc.1993.2229.
It has been previously proposed that the rabbit p59-HBI (Heat shock protein Binding Immunophilin) or rFKBP59 (FK506 Binding Protein), found associated with the 90 kDa heat shock protein in nontransformed steroid receptor complexes, has three domains structurally related to hFKBP12 (Callebaut, I., Renoir, J.M., Lebeau, M.C., Massol, N., Burny, A., Baulieu, E.E. and Mornon, J.P. (1992) Proc. Natl. Acad. Sci., USA 89, 6270-6274). Here we report the overexpression, as fusion proteins in E. coli, of the full length p59-HBI and a series of p59-HBI mutants delimiting these domains and their respective peptidyl prolyl cis trans isomerase (PPlase) activity. The PPlase activity of p59-HBI is comparable to that of hFKBP12 and is due to domain p59-HBI I which displays the highest homology with this immunophilin. The residual enzymatic activity found in domain p59-HBI II is discussed.
先前有人提出，在未转化的类固醇受体复合物中发现的兔p59-HBI（热休克蛋白结合亲免蛋白）或rFKBP59（FK506结合蛋白）与90 kDa热休克蛋白相关，它有三个结构域与hFKBP12相关（卡勒博，I.，勒努瓦，J.M.，勒博，M.C.，马索尔，N.，布尔尼，A.，鲍利厄，E.E.和莫农，J.P.（1992年）《美国国家科学院院刊》89，6270 - 6274）。在此我们报告全长p59-HBI以及一系列界定这些结构域的p59-HBI突变体作为融合蛋白在大肠杆菌中的过表达及其各自的肽基脯氨酰顺反异构酶（PPlase）活性。p59-HBI的PPlase活性与hFKBP12相当，并且是由于p59-HBI I结构域，该结构域与这种亲免蛋白具有最高的同源性。文中讨论了在p59-HBI II结构域中发现的残余酶活性。
