dc.contributor.author | Grøsvik, Kristin | |
dc.contributor.author | Tesfahun, Almaz Nigatu | |
dc.contributor.author | Muruzábal-Lecumberri, Izaskun | |
dc.contributor.author | Haugland, Gyri Teien | |
dc.contributor.author | Leiros, Ingar | |
dc.contributor.author | Ruoff, Peter | |
dc.contributor.author | Kvaløy, Jan Terje | |
dc.contributor.author | Knævelsrud, Ingeborg | |
dc.contributor.author | Ånensen, Hilde | |
dc.contributor.author | Alexeeva, Marina | |
dc.contributor.author | Sato, Kousuke | |
dc.contributor.author | Matsuda, Akira | |
dc.contributor.author | Alseth, Ingrun | |
dc.contributor.author | Klungland, Arne | |
dc.contributor.author | Bjelland, Svein | |
dc.date.accessioned | 2021-03-11T13:40:45Z | |
dc.date.available | 2021-03-11T13:40:45Z | |
dc.date.created | 2020-02-10T01:56:13Z | |
dc.date.issued | 2020 | |
dc.Published | Frontiers in Microbiology. 2020, 11:263 1-17. | |
dc.identifier.issn | 1664-302X | |
dc.identifier.uri | https://hdl.handle.net/11250/2732931 | |
dc.description.abstract | The 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.iso | eng | en_US |
dc.publisher | Frontiers Media | en_US |
dc.rights | Navngivelse 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/deed.no | * |
dc.title | The Escherichia coli alkA Gene Is Activated to Alleviate Mutagenesis by an Oxidized Deoxynucleoside | en_US |
dc.type | Journal article | en_US |
dc.type | Peer reviewed | en_US |
dc.description.version | publishedVersion | en_US |
dc.rights.holder | Copyright 2020 Grøsvik, Tesfahun, Muruzábal-Lecumberri, Haugland, Leiros,Ruoff, Kvaløy, Knævelsrud, Ånensen, Alexeeva, Sato, Matsuda, Alseth, Klungland and Bjelland. | en_US |
dc.source.articlenumber | 263 | en_US |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 2 | |
dc.identifier.doi | 10.3389/fmicb.2020.00263 | |
dc.identifier.cristin | 1792427 | |
dc.source.journal | Frontiers in Microbiology | en_US |
dc.source.40 | 11:263 | |
dc.identifier.citation | Frontiers in Microbiology. 2020, 11, 263. | en_US |
dc.source.volume | 11 | en_US |