ON THE LOCALIZATION OF FKBP25 IN T-LYMPHOCYTES
ON THE LOCALIZATION OF FKBP25 IN T-LYMPHOCYTES
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DOI：
10.1016/0014-5793(93)81173-w
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发表时间：
1993-01-11
期刊：
影响因子：
3.5
通讯作者：
GALAT, A
中科院分区：
文献类型：
--
作者：
RIVIERE, S;MENEZ, A;GALAT, A
利用兔抗牛FKBP25多克隆抗体、NEPHGE/SDS-PAGE和Western blotting，我们证实雷帕霉素特异性免疫亲和蛋白FKBP25存在于t -淋巴瘤Jurkat细胞中。随后对可溶性Jurkat细胞蛋白的分离表明，FKBP25主要发生在细胞核部分。FKBP25具有与DNA结合的能力。FKBP25/DNA复合物可以在高盐浓度下解离。FKBP12与FKBP25的c端结构域具有较高的氨基酸序列同源性，不具有与DNA结合的倾向。对FKBP25二级结构的cd约束预测表明，两亲性螺旋-环-螺旋发生在蛋白质的n端部分，并可能解释其与DNA的结合。
Using polyclonal rabbit antibodies against bovine FKBP25, NEPHGE/SDS-PAGE and Western blotting we demonstrate that the rapamycin-specific immunophilin FKBP25 is present in T-lymphoma Jurkat cells. Subsequent fractionations of the soluble Jurkat cell proteins have revealed that FKBP25 predominantly occurs in the nuclear fraction. FKBP25 has the ability to bind to DNA. The FKBP25/DNA complex can be dissociated in the presence of a high salt concentration. FKBP12, which shares high amino acid sequence homology to the C-terminal domain of FKBP25, has no tendency to bind to DNA. CD-constrained predictions of the secondary structures in FKBP25 suggest that an amphipathic helix-loop-helix occurs in the N-terminal part of the protein and may account for its binding to DNA.