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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Cell Line, Tumor
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Chromatin / genetics
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Gene Silencing*
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Histone Methyltransferases
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Histone-Lysine N-Methyltransferase*
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Humans
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Interferon-beta / genetics
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Macromolecular Substances
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Methyltransferases / metabolism*
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Molecular Sequence Data
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Positive Regulatory Domain I-Binding Factor 1
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Protein Methyltransferases
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Protein Transport
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Repressor Proteins / physiology*
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Substrate Specificity
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Transcription Factors / physiology*
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Transcription, Genetic
Substances
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Chromatin
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Macromolecular Substances
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Prdm1 protein, mouse
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Repressor Proteins
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Transcription Factors
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PRDM1 protein, human
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Interferon-beta
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Histone Methyltransferases
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Methyltransferases
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Positive Regulatory Domain I-Binding Factor 1
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Protein Methyltransferases
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Histone-Lysine N-Methyltransferase