The FK506‐binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1

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.

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