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

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Title:	The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1
Authors:	Yang WM;Yao YL;Seto E
Contributors:	Department of Biotechnology
Keywords:	FK506-binding protein;histone deacetylase;peptidylprolyl cistrans isomerase;transcription factor YY1
Date:	2001-09
Issue Date:	2010-03-15 08:11:17 (UTC+0)
Publisher:	Asia University
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 20(17):4814-25
Appears in Collections:	[Department of Biotechnology] Journal Article

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