The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1
The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1
复制标题
DOI：
10.1093/emboj/20.17.4814
复制
发表时间：
2001-09-03
期刊：
影响因子：
11.4
通讯作者：
Seto, E
中科院分区：
文献类型：
--
作者：
Yang, WM;Yao, YL;Seto, E
FK506结合蛋白(FKBPs)是一类免疫抑制剂的细胞受体，属于免疫亲和素，具有肽基脯氨酰顺式-反式异构酶(PPIase)活性。序列比较表明，HD2型组蛋白脱乙酰酶和FKBP型PPIase可能是由一个共同的祖先酶进化而来。在这里，我们表明FKBP25物理上与组蛋白去乙酰基酶HDAC1和HDAC2以及HDAC结合的转录调控因子YY1有关。FKBP25免疫沉淀复合体含有脱乙酰酶活性，该活性与FKBP25的N-末端相关，不同于FK506/雷帕霉素结合域。此外，FKBP25还可以改变YY1的DNA结合活性。总之，我们的数据确定了组蛋白脱乙酰酶和FKBP酶之间的关系，并为FKBP提供了一个新的关键功能。
FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants that belong to a subgroup of proteins, known as immunophilins, with peptidylprolyl cis-trans isomerase (PPIase) activity. Sequence comparison suggested that the HD2-type histone deacetylases and the FKBP-type PPIases may have evolved from a common ancestor enzyme. Here we show that FKBP25 physically associates with the histone deacetylases HDAC1 and HDAC2 and with the HDAC-binding transcriptional regulator YY1. An FKBP25 immunoprecipitated complex contains deacetylase activity, and this activity is associated with the N-terminus of FKBP25, distinct from the FK506/rapamycin-binding domain. Furthermore, FKBP25 can alter the DNA-binding activity of YY1. Together, our data firmly establish a relationship between histone deacetylases and the FKBP enzymes and provide a novel and critical function for the FKBPs.