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dc.contributor.authorGrøsvik, Kristin
dc.contributor.authorTesfahun, Almaz Nigatu
dc.contributor.authorMuruzábal-Lecumberri, Izaskun
dc.contributor.authorHaugland, Gyri Teien
dc.contributor.authorLeiros, Ingar
dc.contributor.authorRuoff, Peter
dc.contributor.authorKvaløy, Jan Terje
dc.contributor.authorKnævelsrud, Ingeborg
dc.contributor.authorÅnensen, Hilde
dc.contributor.authorAlexeeva, Marina
dc.contributor.authorSato, Kousuke
dc.contributor.authorMatsuda, Akira
dc.contributor.authorAlseth, Ingrun
dc.contributor.authorKlungland, Arne
dc.contributor.authorBjelland, Svein
dc.date.accessioned2020-06-09T07:32:32Z
dc.date.available2020-06-09T07:32:32Z
dc.date.issued2020-02-25
dc.description.abstractThe cellular methyl donor S-adenosylmethionine (SAM) and other endo/exogenous agents methylate DNA bases non-enzymatically into products interfering with replication and transcription. An important product is 3-methyladenine (m<sup>3</sup>A), which in <i>Escherichia coli</i> is removed by m<sup>3</sup>A-DNA glycosylase I (Tag) and II (AlkA). The <i>tag</i> gene is constitutively expressed, while <i>alkA</i> is induced by sub-lethal concentrations of methylating agents. We previously found that AlkA exhibits activity for the reactive oxygen-induced thymine (T) lesion 5-formyluracil (fU) <i>in vitro</i>. Here, we provide evidence for AlkA involvement in the repair of oxidized bases by showing that the adenine (A) ⋅ T → guanine (G) ⋅ cytosine (C) mutation rate increased 10-fold in <i>E. coli</i> wild-type and <i>alkA</i>– cells exposed to 0.1 mM 5-formyl-2′-deoxyuridine (fdU) compared to a wild-type specific reduction of the mutation rate at 0.2 mM fdU, which correlated with <i>alkA</i> gene induction. G⋅C → A⋅T alleviation occurred without <i>alkA</i> induction (at 0.1 mM fdU), correlating with a much higher AlkA efficiency for fU opposite to G than for that to A. The common keto form of fU is the AlkA substrate. Mispairing with G by ionized fU is favored by its exclusion from the AlkA active site.en_US
dc.identifier.citationGrøsvik K, Tesfahun AN, Muruzábal-Lecumberri I, Haugland GT, Leiros I, Ruoff P, Kvaløy JT, Knævelsrud I, Ånensen H, Alexeeva M, Sato, Matsuda A, Alseth I, Klungland A, Bjelland S. The escherichia coli alkA gene is activated to alleviate mutagenesis by an oxidized deoxynucleoside. Frontiers in Microbiology. 2020;11:263:1-17en_US
dc.identifier.cristinIDFRIDAID 1792427
dc.identifier.doi10.3389/fmicb.2020.00263
dc.identifier.issn1664-302X
dc.identifier.urihttps://hdl.handle.net/10037/18488
dc.language.isoengen_US
dc.publisherFrontiers Mediaen_US
dc.relation.journalFrontiers in Microbiology
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2020 The Author(s)en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.subjectVDP::Medical disciplines: 700::Basic medical, dental and veterinary science disciplines: 710en_US
dc.subjectVDP::Medisinske Fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710en_US
dc.titleThe escherichia coli alkA gene is activated to alleviate mutagenesis by an oxidized deoxynucleosideen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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