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"name": {
"name": "Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein D4, Nitratifractor salsuginis UNG and similar proteins",
"short": "UDG-F1-like"
},
"description": [
{
"text": "<p>Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. More distant members of UDG family 1 include Nitratifractor salsuginis UNG (NsaUNG) and Vaccinia virus (VAVC) protein D4 uracil-DNA glycosylase, a subunit of the VACV DNA polymerase holoenzyme. NsaUNG only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates; it does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. D4, in addition to excising uracil residues from DNA, is part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. [[cite:PUB00095188], [cite:PUB00080609], [cite:PUB00000916], [cite:PUB00004202], [cite:PUB00107445], [cite:PUB00080610], [cite:PUB00047227], [cite:PUB00080618], [cite:PUB00080611], [cite:PUB00017590], [cite:PUB00107446], [cite:PUB00080617], [cite:PUB00107447], [cite:PUB00107448], [cite:PUB00127179], [cite:PUB00127180], [cite:PUB00107444]]</p>",
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"issue": "6514",
"year": 1995,
"title": "The structural basis of specific base-excision repair by uracil-DNA glycosylase.",
"URL": null,
"raw_pages": "487-93",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Savva R",
"McAuley-Hecht K",
"Brown T",
"Pearl L."
],
"DOI_URL": "http://dx.doi.org/10.1038/373487a0"
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"PUB00107446": {
"PMID": 4610583,
"ISBN": null,
"volume": "71",
"issue": "9",
"year": 1974,
"title": "An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues.",
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"raw_pages": "3649-53",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc Natl Acad Sci U S A",
"authors": [
"Lindahl T."
],
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"volume": "21",
"issue": "58",
"year": 2002,
"title": "Uracil in DNA--occurrence, consequences and repair.",
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"raw_pages": "8935-48",
"medline_journal": "Oncogene",
"ISO_journal": "Oncogene",
"authors": [
"Krokan HE",
"Drablos F",
"Slupphaug G."
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"DOI_URL": "http://dx.doi.org/10.1038/sj.onc.1205996"
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"issue": "1",
"year": 2001,
"title": "Uracil DNA glycosylase: insights from a master catalyst.",
"URL": null,
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"medline_journal": "Arch Biochem Biophys",
"ISO_journal": "Arch. Biochem. Biophys.",
"authors": [
"Stivers JT",
"Drohat AC."
],
"DOI_URL": "http://dx.doi.org/10.1006/abbi.2001.2605"
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"issue": "3-4",
"year": 2000,
"title": "Lessons learned from structural results on uracil-DNA glycosylase.",
"URL": null,
"raw_pages": "183-99",
"medline_journal": "Mutat Res",
"ISO_journal": "Mutat Res",
"authors": [
"Parikh SS",
"Putnam CD",
"Tainer JA."
],
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},
"PUB00127180": {
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"volume": "589",
"issue": "19 Pt B",
"year": 2015,
"title": "Crystal structure of family 4 uracil-DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding.",
"URL": null,
"raw_pages": "2675-82",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett",
"authors": [
"Kawai A",
"Higuchi S",
"Tsunoda M",
"Nakamura KT",
"Yamagata Y",
"Miyamoto S."
],
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"PMID": 7697717,
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"issue": "6",
"year": 1995,
"title": "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis.",
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"raw_pages": "869-78",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Mol CD",
"Arvai AS",
"Slupphaug G",
"Kavli B",
"Alseth I",
"Krokan HE",
"Tainer JA."
],
"DOI_URL": "http://dx.doi.org/10.1016/0092-8674(95)90290-2"
},
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"PMID": 10946227,
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"title": "Structure and function in the uracil-DNA glycosylase superfamily.",
"URL": null,
"raw_pages": "165-81",
"medline_journal": "Mutat Res",
"ISO_journal": "Mutat. Res.",
"authors": [
"Pearl LH."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0921-8777(00)00025-2"
},
"PUB00107444": {
"PMID": 28977725,
"ISBN": null,
"volume": "284",
"issue": "23",
"year": 2017,
"title": "An unconventional family 1 uracil DNA glycosylase in Nitratifractor salsuginis.",
"URL": null,
"raw_pages": "4017-4034",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J",
"authors": [
"Li J",
"Chen R",
"Yang Y",
"Zhang Z",
"Fang GC",
"Xie W",
"Cao W."
],
"DOI_URL": null
},
"PUB00107447": {
"PMID": 9224623,
"ISBN": null,
"volume": "325 ( Pt 1)",
"issue": null,
"year": 1997,
"title": "DNA glycosylases in the base excision repair of DNA.",
"URL": null,
"raw_pages": "1-16",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem J",
"authors": [
"Krokan HE",
"Standal R",
"Slupphaug G."
],
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},
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"issue": "3",
"year": 2003,
"title": "Crystal structure of a family 4 uracil-DNA glycosylase from Thermus thermophilus HB8.",
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"raw_pages": "515-26",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Hoseki J",
"Okamoto A",
"Masui R",
"Shibata T",
"Inoue Y",
"Yokoyama S",
"Kuramitsu S."
],
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"title": "Phylogenomic analysis of the uracil-DNA glycosylase superfamily.",
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"medline_journal": "Mol Biol Evol",
"ISO_journal": "Mol. Biol. Evol.",
"authors": [
"Lucas-Lledo JI",
"Maddamsetti R",
"Lynch M."
],
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"volume": "373",
"issue": "4",
"year": 2007,
"title": "Crystal structure of family 5 uracil-DNA glycosylase bound to DNA.",
"URL": null,
"raw_pages": "839-50",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Kosaka H",
"Hoseki J",
"Nakagawa N",
"Kuramitsu S",
"Masui R."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2007.08.022"
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"PUB00107448": {
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"volume": "20",
"issue": "10",
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"title": "Mismatch repair: mechanisms and relationship to cancer susceptibility.",
"URL": null,
"raw_pages": "397-401",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem Sci",
"authors": [
"Kolodner RD."
],
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},
"PUB00095188": {
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"ISBN": null,
"volume": "45",
"issue": "10",
"year": 2017,
"title": "Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.",
"URL": null,
"raw_pages": "5863-5876",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Chembazhi UV",
"Patil VV",
"Sah S",
"Reeve W",
"Tiwari RP",
"Woo E",
"Varshney U."
],
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"volume": "685",
"issue": "1-2",
"year": 2010,
"title": "Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition.",
"URL": null,
"raw_pages": "11-20",
"medline_journal": "Mutat Res",
"ISO_journal": "Mutat. Res.",
"authors": [
"Zharkov DO",
"Mechetin GV",
"Nevinsky GA."
],
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"title": "Correlated Mutation in the Evolution of Catalysis in Uracil DNA Glycosylase Superfamily.",
"URL": null,
"raw_pages": "45978",
"medline_journal": "Sci Rep",
"ISO_journal": "Sci Rep",
"authors": [
"Xia B",
"Liu Y",
"Guevara J",
"Li J",
"Jilich C",
"Yang Y",
"Wang L",
"Dominy BN",
"Cao W."
],
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}
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