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PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing.

PRDI-BF1, the human ortholog of mouse Blimp-1, is a DNA-binding protein involved in postinduction repression of interferon-beta gene transcription in response to viral infection. PRDI-BF1 also has an essential function in driving terminal differentiation of B lymphocytes and therein silences multiple genes. Here we show PRDI-BF1 assembles silent chromatin over the interferon-beta promoter in the osteosarcoma cell line U2OS through recruitment of the histone H3 lysine methyltransferase G9a. G9a is recruited only when in a complex with PRDI-BF1. G9a catalytic activity is required for the accumulation of methylated histone H3 and transcriptional silencing mediated by PRDI-BF1 in vivo. This establishes a mechanism for the recruitment of G9a, the main mammalian euchromatic methyltransferase, and defines nonembryonic targets of G9a.

Pubmed ID: 14985713


  • Gyory I
  • Wu J
  • Fej√©r G
  • Seto E
  • Wright KL


Nature immunology

Publication Data

March 26, 2004

Associated Grants

  • Agency: NCI NIH HHS, Id: CA 80990

Mesh Terms

  • Amino Acid Sequence
  • Cell Line, Tumor
  • Chromatin
  • Gene Silencing
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Interferon-beta
  • Macromolecular Substances
  • Methyltransferases
  • Molecular Sequence Data
  • Protein Methyltransferases
  • Protein Transport
  • Repressor Proteins
  • Substrate Specificity
  • Transcription Factors
  • Transcription, Genetic