論文

国際誌
2021年4月

Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase.

Life science alliance
  • Cheng-Han Ho
  • ,
  • Yoshimasa Takizawa
  • ,
  • Wataru Kobayashi
  • ,
  • Yasuhiro Arimura
  • ,
  • Hiroshi Kimura
  • ,
  • Hitoshi Kurumizaka

4
4
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.26508/lsa.202000919

SET8 is solely responsible for histone H4 lysine-20 (H4K20) monomethylation, which preferentially occurs in nucleosomal H4. However, the underlying mechanism by which SET8 specifically promotes the H4K20 monomethylation in the nucleosome has not been elucidated. Here, we report the cryo-EM structures of the human SET8-nucleosome complexes with histone H3 and the centromeric H3 variant, CENP-A. Surprisingly, we found that the overall cryo-EM structures of the SET8-nucleosome complexes are substantially different from the previous crystal structure models. In the complexes with H3 and CENP-A nucleosomes, SET8 specifically binds the nucleosomal acidic patch via an arginine anchor, composed of the Arg188 and Arg192 residues. Mutational analyses revealed that the interaction between the SET8 arginine anchor and the nucleosomal acidic patch plays an essential role in the H4K20 monomethylation activity. These results provide the groundwork for understanding the mechanism by which SET8 specifically accomplishes the H4K20 monomethylation in the nucleosome.

リンク情報
DOI
https://doi.org/10.26508/lsa.202000919
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/33574035
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7893823
ID情報
  • DOI : 10.26508/lsa.202000919
  • PubMed ID : 33574035
  • PubMed Central 記事ID : PMC7893823

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