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)

抄録

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.

本文言語英語
ページ(範囲)227-241
ページ数15
ジャーナルGenes and Genetic Systems
77
4
DOI
出版ステータス出版済み - 8 2002

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

フィンガープリント 「Novel endonuclease in archaea cleaving DNA with various branched structure」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル