Methyl-CpG Binding Domain 1 (MBD1) Interacts with the Suv39h1-HP1 Heterochromatic Complex for DNA Methylation-based Transcriptional Repression

We show that histone H3 methylase Suv39h1 and the methyl lysine-binding protein HP1 directly interact with methylCpG binding domain of MBD1 in vitro and in cells

Naoyuki Fujita; Sugiko Watanabe; Takaya Ichimura; Shu Tsuruzoe; Yoichi Shinkai; Makoto Tachibana; Tsutomu Chiba; Mitsuyoshi Nakao

2003

Scholarcy highlights

  • DNA and protein modifications create a new surface for interaction with target molecules
  • During investigation of the mechanism of transcriptional repression by the transcriptional repression domain of MBD1, we have recently found that a transcriptional mediator, MBD1containing chromatin associated factor, binds the TRD of MBD1 to form the repressive complex
  • Localization of MBD1, Suv39h1, G9a, and HP1␣ in the Nucleus—To address the mechanism(s) of transcriptional repression by MBD1, we considered whether MBD1 can associate with histone methylases such as Suv39h1 and G9a by using an immunofluorescence analysis in HeLa cells
  • As previous reports demonstrated that Suv39h1 associates with HP1␣, MBD1 was found to mostly coexist with HP1␣
  • We report that Suv39h1 and HP1␣ interact with MBD1
  • The localization of Suv39h1, HP1␣, and HDACs onto MBD1-containing methylated DNA sites may exemplify the possible presence of a repression pathway from DNA methylation to these histone modifications in heterochromatic regions

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