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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/16985


    Title: The FK506-binding protein 25 functionally associates with histone deacetylases and transcription factor YY1
    Authors: 姚雅莉;Yao, Ya-Li
    Contributors: 生物科技學系
    Keywords: FK506-binding protein;histone deacetylase/peptidylprolyl cis–trans isomerase;transcription factor YY1
    Date: 2001-09
    Issue Date: 2012-11-23 17:19:06 (UTC+8)
    Abstract: 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.
    Relation: EMBO JOURNAL
    Appears in Collections:[生物科技學系] 期刊論文

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