Novel endonuclease in archaea cleaving DNA with various branched structure

Kayoko Komori, Ryosuke Fujikane, Hideo Shinagawa, Yoshizumi Ishino

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)227-241
Number of pages15
JournalGenes and Genetic Systems
Volume77
Issue number4
DOIs
Publication statusPublished - Aug 1 2002

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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