Novel endonuclease in archaea cleaving DNA with various branched structure

Kayoko Komori, Ryosuke Fujikane, Hideo Shinagawa, Yoshizumi Ishino

研究成果: Contribution to journalArticle査読

73 被引用数 (Scopus)


We identified a novel structure-specific endonuclease in Pyrococcus furiosus. This nuclease contains two distinct domains, which are similar to the DEAH helicase family at the N-terminal two-third and the XPF endonuclease superfamily at the C-terminal one-third of the protein, respectively. The C-terminal domain has an endonuclease activity cleaving the DNA strand at the 5′-side of nicked or flapped positions in the duplex DNA. The nuclease also incises in the proximity of the 5′-side of a branch point in the template strand for leading synthesis in the fork-structured DNA. The N-terminal helicase may work cooperatively to change the fork structure suitable for cleavage by the C-terminal endonuclease. This protein, designated as Hef (helicase-associated endonuclease for fork-structured DNA), may be a prototypical enzyme for resolving stalled forks during DNA replication, as well as working at nucleotide excision repair.

ジャーナルGenes and Genetic Systems
出版ステータス出版済み - 8 2002

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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