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    Nat Immunol. 2004 Mar;5(3):299-308. Epub 2004 Feb 22.

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

    Gyory I, Wu J, Fejér G, Seto E, Wright KL.

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    Department of Biochemistry and Molecular Biology, H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, 12902 Magnolia Drive, MRC4East, Tampa, FL 33612, USA.

    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.

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    PMID:
    14985713
    [PubMed - indexed for MEDLINE]

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