{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1362262944832819072.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.0908307107"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.0908307107"}}],"dc:title":[{"@value":"The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n            To protect cells from oxidative DNA damage and mutagenesis, organisms possess multiple glycosylases to recognize the damaged bases and to initiate the Base Excision Repair pathway. Three DNA glycosylases have been identified in mammals that are homologous to the\n            <jats:italic>Escherichia coli</jats:italic>\n            Fpg and Nei proteins, Neil1, Neil2, and Neil3. Neil1 and Neil2 in human and mouse have been well characterized while the properties of the Neil3 protein remain to be elucidated. In this study, we report the characterization of\n            <jats:italic>Mus musculus</jats:italic>\n            (house mouse) Neil3 (MmuNeil3) as an active DNA glycosylase both in vitro and in vivo. In duplex DNA, MmuNeil3 recognizes the oxidized purines, spiroiminodihydantoin (Sp), guanidinohydantoin (Gh), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino- 5-formamidopyrimidine (FapyA), but not 8-oxo-7,8-dihydroguanine (8-oxoG). Interestingly, MmuNeil3 prefers lesions in single-stranded DNA and in bubble structures. In contrast to other members of the family that use the N-terminal proline as the nucleophile, MmuNeil3 forms a Schiff base intermediate via its N-terminal valine. We expressed the glycosylase domain of MmuNeil3 (MmuNeil3Δ324) in an\n            <jats:italic>Escherichia coli</jats:italic>\n            triple mutant lacking Fpg, Nei, and MutY glycosylase activities and showed that MmuNeil3 greatly reduced both the spontaneous mutation frequency and the level of FapyG in the DNA, suggesting that Neil3 plays a role in repairing FapyG in vivo.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380576149352590464","@type":"Researcher","foaf:name":[{"@value":"Minmin Liu"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0086;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590470","@type":"Researcher","foaf:name":[{"@value":"Viswanath Bandaru"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0086;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590467","@type":"Researcher","foaf:name":[{"@value":"Jeffrey P. Bond"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0086;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590469","@type":"Researcher","foaf:name":[{"@value":"Pawel Jaruga"}],"jpcoar:affiliationName":[{"@value":"Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Building 227/A243, Gaithersburg, MD 20899;"},{"@value":"Department of Clinical Biochemistry, Collegium Medicum, Nicolaus Copernicus University, Bydgoszcz, Poland;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590473","@type":"Researcher","foaf:name":[{"@value":"Xiaobei Zhao"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry, University of Utah, Salt Lake City, UT 84112-0850; and"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590472","@type":"Researcher","foaf:name":[{"@value":"Plamen P. Christov"}],"jpcoar:affiliationName":[{"@value":"Departments of Chemistry and Biochemistry and Center in Molecular Toxicology, Vanderbilt University, Nashville, TN 37235-1822"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590466","@type":"Researcher","foaf:name":[{"@value":"Cynthia J. Burrows"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry, University of Utah, Salt Lake City, UT 84112-0850; and"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590468","@type":"Researcher","foaf:name":[{"@value":"Carmelo J. Rizzo"}],"jpcoar:affiliationName":[{"@value":"Departments of Chemistry and Biochemistry and Center in Molecular Toxicology, Vanderbilt University, Nashville, TN 37235-1822"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590471","@type":"Researcher","foaf:name":[{"@value":"Miral Dizdaroglu"}],"jpcoar:affiliationName":[{"@value":"Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Building 227/A243, Gaithersburg, MD 20899;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576149352590465","@type":"Researcher","foaf:name":[{"@value":"Susan S. Wallace"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0086;"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2010-02-25","prism:volume":"107","prism:number":"11","prism:startingPage":"4925","prism:endingPage":"4930"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.0908307107"}],"createdAt":"2010-02-26","modifiedAt":"2022-04-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050304394133443200","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"NEIL1: The second DNA glycosylase involved in action-at-a-distance mutations induced by 8-oxo-7,8-dihydroguanine"}]},{"@id":"https://cir.nii.ac.jp/crid/1050861770482354944","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002218674153088","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Abnormal Expressions of DNA Glycosylase Genes NEIL1, NEIL2, and NEIL3 Are Associated with Somatic Mutation Loads in Human Cancer"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004234671173120","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Restriction-modification system with methyl-inhibited base excision and abasic-site cleavage activities"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1073/pnas.0908307107"},{"@type":"CROSSREF","@value":"10.1155/2016/1546392_references_DOI_U6yJAJ84gJeYaVVl7o9WuRsqlGj"},{"@type":"CROSSREF","@value":"10.1093/nar/gkv116_references_DOI_U6yJAJ84gJeYaVVl7o9WuRsqlGj"},{"@type":"CROSSREF","@value":"10.1016/j.freeradbiomed.2025.01.041_references_DOI_U6yJAJ84gJeYaVVl7o9WuRsqlGj"},{"@type":"CROSSREF","@value":"10.1186/s41021-023-00266-5_references_DOI_U6yJAJ84gJeYaVVl7o9WuRsqlGj"}]}