Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity

J Biol Chem. 1995 Jun 23;270(25):15187-93. doi: 10.1074/jbc.270.25.15187.

Abstract

YY1 is a zinc finger transcription factor with unusual structural and functional features. In a yeast two-hybrid screen, two cellular proteins, cyclophilin A (CyPA) and FK506-binding protein 12 (FKBP12), interacted with YY1. These interactions are specific and also occur in mammalian cells. Cyclosporin A and FK506 efficiently disrupt the YY1-CyPA and YY1-FKBP12 interactions. Overexpression of human CyPA and FKBP12 have different effects on YY1-regulated transcription with these effects being promoter-dependent. These results suggest that immunophilins may be mediators in the functional role of YY1.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Isomerases / metabolism*
  • Carrier Proteins / metabolism*
  • Chloramphenicol O-Acetyltransferase / metabolism
  • Cyclosporine / pharmacology
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases / metabolism
  • Erythroid-Specific DNA-Binding Factors
  • HeLa Cells
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Peptidylprolyl Isomerase
  • Promoter Regions, Genetic
  • Recombinant Fusion Proteins / metabolism
  • TATA Box
  • Tacrolimus / pharmacology
  • Tacrolimus Binding Proteins
  • Transcription Factors / metabolism*
  • Transcription, Genetic* / drug effects
  • Transfection
  • YY1 Transcription Factor
  • Zinc Fingers

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • Erythroid-Specific DNA-Binding Factors
  • Heat-Shock Proteins
  • Recombinant Fusion Proteins
  • Transcription Factors
  • YY1 Transcription Factor
  • YY1 protein, human
  • Cyclosporine
  • Chloramphenicol O-Acetyltransferase
  • Endodeoxyribonucleases
  • Amino Acid Isomerases
  • Tacrolimus Binding Proteins
  • Peptidylprolyl Isomerase
  • Tacrolimus