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- W2064577894 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." @default.
- W2064577894 created "2016-06-24" @default.
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- W2064577894 date "2002-01-01" @default.
- W2064577894 modified "2023-09-30" @default.
- W2064577894 title "Novel endonuclease in Archaea cleaving DNA with various branched structure." @default.
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- W2064577894 doi "https://doi.org/10.1266/ggs.77.227" @default.
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