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

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)899-904
Number of pages6
JournalJournal of Biological Chemistry
Volume295
Issue number4
DOIs
Publication statusPublished - Jan 24 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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