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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.accessioned2021-03-11T13:40:45Z
dc.date.available2021-03-11T13:40:45Z
dc.date.created2020-02-10T01:56:13Z
dc.date.issued2020
dc.PublishedFrontiers in Microbiology. 2020, 11:263 1-17.
dc.identifier.issn1664-302X
dc.identifier.urihttps://hdl.handle.net/11250/2732931
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 (m3A), which in Escherichia coli is removed by m3A-DNA glycosylase I (Tag) and II (AlkA). The tag gene is constitutively expressed, while alkA 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) in vitro. 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 E. coli wild-type and alkA– 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 alkA gene induction. G⋅C → A⋅T alleviation occurred without alkA 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.language.isoengen_US
dc.publisherFrontiers Mediaen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleThe Escherichia coli alkA Gene Is Activated to Alleviate Mutagenesis by an Oxidized Deoxynucleosideen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2020 Grøsvik, Tesfahun, Muruzábal-Lecumberri, Haugland, Leiros,Ruoff, Kvaløy, Knævelsrud, Ånensen, Alexeeva, Sato, Matsuda, Alseth, Klungland and Bjelland.en_US
dc.source.articlenumber263en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.doi10.3389/fmicb.2020.00263
dc.identifier.cristin1792427
dc.source.journalFrontiers in Microbiologyen_US
dc.source.4011:263
dc.identifier.citationFrontiers in Microbiology. 2020, 11, 263.en_US
dc.source.volume11en_US


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