論文

査読有り 国際誌
2019年10月4日

H3K14 ubiquitylation promotes H3K9 methylation for heterochromatin assembly.

EMBO reports
  • Eriko Oya
  • ,
  • Reiko Nakagawa
  • ,
  • Yuriko Yoshimura
  • ,
  • Mayo Tanaka
  • ,
  • Gohei Nishibuchi
  • ,
  • Shinichi Machida
  • ,
  • Atsuko Shirai
  • ,
  • Karl Ekwall
  • ,
  • Hitoshi Kurumizaka
  • ,
  • Hideaki Tagami
  • ,
  • Jun-Ichi Nakayama

20
10
開始ページ
e48111
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.15252/embr.201948111
出版者・発行元
EMBO Press

The methylation of histone H3 at lysine 9 (H3K9me), performed by the methyltransferase Clr4/SUV39H, is a key event in heterochromatin assembly. In fission yeast, Clr4, together with the ubiquitin E3 ligase Cul4, forms the Clr4 methyltransferase complex (CLRC), whose physiological targets and biological role are currently unclear. Here, we show that CLRC-dependent H3 ubiquitylation regulates Clr4's methyltransferase activity. Affinity-purified CLRC ubiquitylates histone H3, and mass spectrometric and mutation analyses reveal that H3 lysine 14 (H3K14) is the preferred target of the complex. Chromatin immunoprecipitation analysis shows that H3K14 ubiquitylation (H3K14ub) is closely associated with H3K9me-enriched chromatin. Notably, the CLRC-mediated H3 ubiquitylation promotes H3K9me by Clr4, suggesting that H3 ubiquitylation is intimately linked to the establishment and/or maintenance of H3K9me. These findings demonstrate a cross-talk mechanism between histone ubiquitylation and methylation that is involved in heterochromatin assembly.

リンク情報
DOI
https://doi.org/10.15252/embr.201948111
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/31468675
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6776926