Crystal structure of the novel lesion-specific endonuclease PfuEndoQ from Pyrococcus furiosus

Ken ichi Miyazono, Sonoko Ishino, Naruto Makita, Tomoko Ito, Yoshizumi Ishino, Masaru Tanokura

研究成果: ジャーナルへの寄稿記事

抄録

Because base deaminations, which are promoted by high temperature, ionizing radiation, aerobic respiration and nitrosative stress, produce mutations during replication, deaminated bases must be repaired quickly to maintain genome integrity. Recently, we identified a novel lesion-specific endonuclease, PfuEndoQ, from Pyrococcus furiosus, and PfuEndoQ may be involved in the DNA repair pathway in Thermococcales of Archaea. PfuEndoQ recognizes a deaminated base and cleaves the phosphodiester bond 5' of the lesion site. To elucidate the structural basis of the substrate recognition and DNA cleavage mechanisms of PfuEndoQ, we determined the structure of PfuEndoQ using X-ray crystallography. The PfuEndoQ structure and the accompanying biochemical data suggest that PfuEndoQ recognizes a deaminated base using a highly conserved pocket adjacent to a Zn2+-binding site and hydrolyses a phosphodiester bond using two Zn2+ ions. The PfuEndoQ-DNA complex is stabilized by a Zn-binding domain and a C-terminal helical domain, and the complex may recruit downstream proteins in the DNA repair pathway.

元の言語英語
ページ(範囲)4807-4818
ページ数12
ジャーナルNucleic acids research
46
発行部数9
DOI
出版物ステータス出版済み - 5 1 2018

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Pyrococcus furiosus
Endonucleases
DNA Repair
Thermococcales
DNA Cleavage
Deamination
X Ray Crystallography
Archaea
Ionizing Radiation
Respiration
Binding Sites
Genome
Ions
Mutation
Temperature
DNA
Proteins

All Science Journal Classification (ASJC) codes

  • Genetics

これを引用

Crystal structure of the novel lesion-specific endonuclease PfuEndoQ from Pyrococcus furiosus. / Miyazono, Ken ichi; Ishino, Sonoko; Makita, Naruto; Ito, Tomoko; Ishino, Yoshizumi; Tanokura, Masaru.

:: Nucleic acids research, 巻 46, 番号 9, 01.05.2018, p. 4807-4818.

研究成果: ジャーナルへの寄稿記事

Miyazono, Ken ichi ; Ishino, Sonoko ; Makita, Naruto ; Ito, Tomoko ; Ishino, Yoshizumi ; Tanokura, Masaru. / Crystal structure of the novel lesion-specific endonuclease PfuEndoQ from Pyrococcus furiosus. :: Nucleic acids research. 2018 ; 巻 46, 番号 9. pp. 4807-4818.
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abstract = "Because base deaminations, which are promoted by high temperature, ionizing radiation, aerobic respiration and nitrosative stress, produce mutations during replication, deaminated bases must be repaired quickly to maintain genome integrity. Recently, we identified a novel lesion-specific endonuclease, PfuEndoQ, from Pyrococcus furiosus, and PfuEndoQ may be involved in the DNA repair pathway in Thermococcales of Archaea. PfuEndoQ recognizes a deaminated base and cleaves the phosphodiester bond 5' of the lesion site. To elucidate the structural basis of the substrate recognition and DNA cleavage mechanisms of PfuEndoQ, we determined the structure of PfuEndoQ using X-ray crystallography. The PfuEndoQ structure and the accompanying biochemical data suggest that PfuEndoQ recognizes a deaminated base using a highly conserved pocket adjacent to a Zn2+-binding site and hydrolyses a phosphodiester bond using two Zn2+ ions. The PfuEndoQ-DNA complex is stabilized by a Zn-binding domain and a C-terminal helical domain, and the complex may recruit downstream proteins in the DNA repair pathway.",
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AU - Miyazono, Ken ichi

AU - Ishino, Sonoko

AU - Makita, Naruto

AU - Ito, Tomoko

AU - Ishino, Yoshizumi

AU - Tanokura, Masaru

PY - 2018/5/1

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N2 - Because base deaminations, which are promoted by high temperature, ionizing radiation, aerobic respiration and nitrosative stress, produce mutations during replication, deaminated bases must be repaired quickly to maintain genome integrity. Recently, we identified a novel lesion-specific endonuclease, PfuEndoQ, from Pyrococcus furiosus, and PfuEndoQ may be involved in the DNA repair pathway in Thermococcales of Archaea. PfuEndoQ recognizes a deaminated base and cleaves the phosphodiester bond 5' of the lesion site. To elucidate the structural basis of the substrate recognition and DNA cleavage mechanisms of PfuEndoQ, we determined the structure of PfuEndoQ using X-ray crystallography. The PfuEndoQ structure and the accompanying biochemical data suggest that PfuEndoQ recognizes a deaminated base using a highly conserved pocket adjacent to a Zn2+-binding site and hydrolyses a phosphodiester bond using two Zn2+ ions. The PfuEndoQ-DNA complex is stabilized by a Zn-binding domain and a C-terminal helical domain, and the complex may recruit downstream proteins in the DNA repair pathway.

AB - Because base deaminations, which are promoted by high temperature, ionizing radiation, aerobic respiration and nitrosative stress, produce mutations during replication, deaminated bases must be repaired quickly to maintain genome integrity. Recently, we identified a novel lesion-specific endonuclease, PfuEndoQ, from Pyrococcus furiosus, and PfuEndoQ may be involved in the DNA repair pathway in Thermococcales of Archaea. PfuEndoQ recognizes a deaminated base and cleaves the phosphodiester bond 5' of the lesion site. To elucidate the structural basis of the substrate recognition and DNA cleavage mechanisms of PfuEndoQ, we determined the structure of PfuEndoQ using X-ray crystallography. The PfuEndoQ structure and the accompanying biochemical data suggest that PfuEndoQ recognizes a deaminated base using a highly conserved pocket adjacent to a Zn2+-binding site and hydrolyses a phosphodiester bond using two Zn2+ ions. The PfuEndoQ-DNA complex is stabilized by a Zn-binding domain and a C-terminal helical domain, and the complex may recruit downstream proteins in the DNA repair pathway.

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