Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing

Tatsuya Nishino, Kayoko Komori, Daisuke Tsuchiya, Yoshizumi Ishino, Kosuke Morikawa

研究成果: ジャーナルへの寄稿学術誌査読

76 被引用数 (Scopus)

抄録

DNA and RNA frequently form various branched intermediates that are important for the transmission of genetic information. Helicases play pivotal roles in the processing of these transient intermediates during nucleic acid metabolism. The archaeal Hef helicase/ nuclease is a representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease family. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. The structure reveals a novel helical insertion between the two conserved helicase core domains. This positively charged extra region, structurally similar to the "thumb" domain of DNA polymerase, plays critical roles in fork recognition. The Hef helicase/nuclease exhibits sequence similarity to the Mph1 helicase from Saccharomyces cerevisiae; XPF/Rad1, involved in DNA repair; and a putative Hef homolog identified in mammals. Hence, our findings provide a structural basis for the functional mechanisms of this helicase/nuclease family.

本文言語英語
ページ(範囲)143-153
ページ数11
ジャーナルStructure
13
1
DOI
出版ステータス出版済み - 1月 2005

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学

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