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

Ildikó Gyory, Jian Wu, György Fejér, Edward Seto, Kenneth L. Wright*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)299-308
Number of pages0
JournalNat Immunol
Volume5
Issue number3
DOIs
Publication statusPublished - Mar 2004

Keywords

  • Amino Acid Sequence
  • Cell Line
  • Tumor
  • Chromatin
  • Gene Silencing
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Interferon-beta
  • Macromolecular Substances
  • Methyltransferases
  • Molecular Sequence Data
  • Positive Regulatory Domain I-Binding Factor 1
  • Protein Methyltransferases
  • Protein Transport
  • Repressor Proteins
  • Substrate Specificity
  • Transcription Factors
  • Transcription
  • Genetic

Fingerprint

Dive into the research topics of 'PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing.'. Together they form a unique fingerprint.

Cite this