Role of Bmi-1 and Ring1A in H2A ubiquitylation and hox gene silencing

Ru Cao, Yu Ichi Tsukada, Yi Zhang

研究成果: ジャーナルへの寄稿学術誌査読

660 被引用数 (Scopus)

抄録

Polycomb group (PcG) proteins exist in at least two biochemically distinct protein complexes, the EED-EZH2 complex and the PRC1 complex, that respectively possess H3-K27 methyltransferase and H2A-K119 ubiquitin E3 ligase activities. How the enzymatic activities are regulated and what their role is in Hox gene silencing are not clear. Here, we demonstrate that Bmi-1 and Ring1A, two components of the PRC1 complex, play important roles in H2A ubiquitylation and Hox gene silencing. We show that both proteins positively regulate H2A ubiquitylation. Chromatin immunoprecipitation (ChIP) assays demonstrate that Bmi-1 and other components of the two PcG complexes bind to the promoter of HoxC13. Knockout Bmi-1 results in significant loss of H2A ubiquitylation and upregulation of Hoxc13 expression, whereas EZH2-mediated H3-K27 methylation is not affected. Our results suggest that EZH2-mediated H3-K27 methylation functions upstream of PRC1 and establishes a critical role for Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.

本文言語英語
ページ(範囲)845-854
ページ数10
ジャーナルMolecular Cell
20
6
DOI
出版ステータス出版済み - 12月 22 2005
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 細胞生物学

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