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The escherichia coli alkA gene is activated to alleviate mutagenesis by an oxidized deoxynucleoside

Permanent link
https://hdl.handle.net/10037/18488
DOI
https://doi.org/10.3389/fmicb.2020.00263
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Date
2020-02-25
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Author
Grøsvik, Kristin; Tesfahun, Almaz Nigatu; Muruzábal-Lecumberri, Izaskun; Haugland, Gyri Teien; Leiros, Ingar; Ruoff, Peter; Kvaløy, Jan Terje; Knævelsrud, Ingeborg; Ånensen, Hilde; Alexeeva, Marina; Sato, Kousuke; Matsuda, Akira; Alseth, Ingrun; Klungland, Arne; Bjelland, Svein
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.
Publisher
Frontiers Media
Citation
Grøsvik 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;11:263:1-17
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