Novel endonuclease in Archaea cleaving DNA with various branched structure
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概要
- 論文の詳細を見る
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.
- 日本遺伝学会の論文
- 2002-08-25
著者
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ISHINO Yoshizumi
Department of Genetic Resources Technology, Faculty of Agriculture, Kyushu University
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Shinagawa Hideo
Department Of Biomedical Sciences University Of Maryland Baltimore
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Komori Kayoko
Department Of Molecular Biology Biomolecular Engineering Research Institute
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FUJIKANE Ryosuke
Department of Molecular Biology, Biomolecular Engineering Research Institute
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Ishino Yoshizumi
Department Of Genetic Resources Technology Graduate School Of Bioresource And Bioenvironmental Scien
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Ishino Yoshizumi
Department Of Molecular Biology Biomolecular Engineering Research Institute
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Fujikane Ryosuke
Department Of Molecular Biology Biomolecular Engineering Research Institute
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Ishino Yoshizumi
Department Of Bioscience And Biotechnology Graduate School Of Bioresource And Bioenvironmental Scien
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