We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1.
- Authors
Wen-ming Yang; Va-Li Vao; Seto, Edward
- Abstract
FK5O6-binding proteins (FKBPs) are cellular receptors for immunosuppressants that belong to a subgroup of proteins, known as immunophilins, with peptidyiprolyl cis-trans isomerase (PPIase) activity. Sequence comparison suggested that the HD2-type histone deacetylases and the FKBP-type PPlases may have evolved from a common ancestor enzyme. Here we show that FKBP2S 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.
- Publication
EMBO Journal, 2001, Vol 20, Issue 17, p4814
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1093/emboj/20.17.4814