Novel endonuclease in Archaea cleaving DNA with various branched structure.
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.
Komori
Kayoko
K
Department of Molecular Biology, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
Fujikane
Ryosuke
R
Shinagawa
Hideo
H
Ishino
Yoshizumi
Y
D000595:Amino Acid Sequence; D004247:DNA / Q000378:metabolism*; D004260:DNA Repair / Q000235:genetics* / Q000502:physiology; D004261:DNA Replication / Q000502:physiology; D004268:DNA-Binding Proteins / Q000235:genetics; D004706:Endodeoxyribonucleases / Q000235:genetics; D004720:Endonucleases / Q000235:genetics* / Q000378:metabolism; D045565:Holliday Junction Resolvases; D008969:Molecular Sequence Data; D020027:Pyrococcus furiosus / Q000201:enzymology / Q000235:genetics*
D004268:DNA-Binding Proteins; D004247:DNA; D004706:Endodeoxyribonucleases; D004720:Endonucleases; D045565:Holliday Junction Resolvases