Structure of the EndoMS-DNA Complex as Mismatch Restriction Endonuclease

Setsu Nakae, Atsushi Hijikata, Toshiyuki Tsuji, Kouki Yonezawa, Ken ichi Kouyama, Kouta Mayanagi, Sonoko Ishino, Yoshizumi Ishino, Tsuyoshi Shirai

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


Archaeal NucS nuclease was thought to degrade the single-stranded region of branched DNA, which contains flapped and splayed DNA. However, recent findings indicated that EndoMS, the orthologous enzyme of NucS, specifically cleaves double-stranded DNA (dsDNA) containing mismatched bases. In this study, we determined the structure of the EndoMS-DNA complex. The complex structure of the EndoMS dimer with dsDNA unexpectedly revealed that the mismatched bases were flipped out into binding sites, and the overall architecture most resembled that of restriction enzymes. The structure of the apo form was similar to the reported structure of Pyrococcus abyssi NucS, indicating that movement of the C-terminal domain from the resting state was required for activity. In addition, a model of the EndoMS-PCNA-DNA complex was preliminarily verified with electron microscopy. The structures strongly support the idea that EndoMS acts in a mismatch repair pathway.

Original languageEnglish
Pages (from-to)1960-1971
Number of pages12
Issue number11
Publication statusPublished - Nov 1 2016

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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