Structure of the RAD9-RAD1-HUS1 checkpoint clamp bound to RHINO sheds light on the other side of the DNA clamp

Kodai Hara, Nao Iida, Ryota Tamafune, Eiji Ohashi, Hitomi Sakurai, Yoshinobu Ishikawa, Asami Hishiki, Hiroshi Hashimoto

研究成果: Contribution to journalArticle査読

1 被引用数 (Scopus)

抄録

DNA clamp, a highly conserved ring-shaped protein, binds dsDNA within its central pore. Also, DNA clamp interacts with various nuclear proteins on its front, thereby stimulating their enzymatic activities and biological functions. It has been assumed that the DNA clamp is a functionally single-faced ring from bacteria to humans. Here, we report the crystal structure of the heterotrimeric RAD9-RAD1-HUS1 (9-1-1) checkpoint clamp bound to a peptide of RHINO, a recently identified cancer- related protein that interacts with 9-1-1 and promotes activation of theDNAdamage checkpoint. This is the first structure of 9-1-1 bound to its partner. The structure reveals that RHINO is unexpectedly bound to the edge and around the back of the 9-1-1 ring through specific interactions with the RAD1 subunit of 9-1-1. Our finding indicates that 9-1-1 is a functionally double- faced DNA clamp.

本文言語英語
ページ(範囲)899-904
ページ数6
ジャーナルJournal of Biological Chemistry
295
4
DOI
出版ステータス出版済み - 1 24 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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