Gyory Ildikó, Wu Jian, Fejér György, Seto Edward, Wright Kenneth L
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.
Nat Immunol. 2004 Mar;5(3):299-308. doi: 10.1038/ni1046. Epub 2004 Feb 22.
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.
PRDI - BF1是小鼠Blimp - 1的人类同源物，是一种DNA结合蛋白，参与病毒感染后干扰素β基因转录的诱导后抑制。PRDI - BF1在驱动B淋巴细胞的终末分化中也具有重要功能，并在此过程中使多个基因沉默。在此我们展示，PRDI - BF1通过募集组蛋白H3赖氨酸甲基转移酶G9a，在骨肉瘤细胞系U2OS的干扰素β启动子上组装沉默染色质。G9a仅在与PRDI - BF1形成复合物时才被募集。在体内，PRDI - BF1介导的甲基化组蛋白H3的积累和转录沉默需要G9a的催化活性。这建立了一种募集主要的哺乳动物常染色质甲基转移酶G9a的机制，并确定了G9a的非胚胎靶点。
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