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 language | English |
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Pages (from-to) | 299-308 |
Number of pages | 0 |
Journal | Nat Immunol |
Volume | 5 |
Issue number | 3 |
DOIs | |
Publication status | Published - 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