Role of mismatch-specific uracil-DNA glycosylase in repair of 3,N4-ethenocytosine in vivo

Jurado, Juan; Maciejewska, Agnieszka; Krwawicz, Joanna; Laval, Jacques; Saparbaev, Murat

doi:10.1016/j.dnarep.2004.06.012

Cited by 22 publications

(15 citation statements)

References 45 publications

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“…It is known that the lesions studied here can be repaired via the base excision repair pathway. The exocyclic adducts ⑀C, HEC, HPC (26,38,39), and to some extent ⑀A (24,40) are excised from DNA by bacterial Mug glycosylase. It has been shown in in vitro experiments that ⑀A is removed from DNA by AlkA glycosylase (41).…”

Section: Discussionmentioning

confidence: 99%

AlkB Dioxygenase Preferentially Repairs Protonated Substrates

Maciejewska

Poznański

Kaczmarska

et al. 2013

Journal of Biological Chemistry

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Background: AlkB dioxygenase removes alkyl and exocyclic lesions via an oxidative mechanism, restoring the native DNA bases. Results: AlkB repair efficiency is pH-and Fe(II) concentration-dependent, which correlates with the substrate pK a . Conclusion: AlkB recognizes and repairs protonated substrates. Significance: This study provides experimental evidence for the molecular mechanism of action of AlkB.

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Section: Discussionmentioning

confidence: 99%

AlkB Dioxygenase Preferentially Repairs Protonated Substrates

Maciejewska

Poznański

Kaczmarska

et al. 2013

Journal of Biological Chemistry

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“…However, Essigmann and coworkers have shown that AlkB is the principal enzyme that removes 1,N 6 -ethenoadenine and 1,N 6 -ethenocytosine (20) as well as 1,N 6 -ethanoadenine (28), adducts that can result from hydroxyl radical lipid peroxidation-mediated DNA damage (25). Other glycosylases that remove oxidized bases include AlkA (7,46), MUG (37,59), KsgA (71), and endonucleases III (55,62) and VIII, encoded by the nth gene (33) and the nei gene (36,48), respectively. Tag, Ogt, and the recently characterized YbzA remove alkylated bases (47), but it is possible that they may also contribute to the removal of as yet unidentified adducts.…”

Section: Figmentioning

confidence: 99%

The Aminoglycoside Antibiotic Kanamycin Damages DNA Bases in Escherichia coli: Caffeine Potentiates the DNA-Damaging Effects of Kanamycin while Suppressing Cell Killing by Ciprofloxacin in Escherichia coli and Bacillus anthracis

Kang¹,

Yuan²,

Nguyen³

et al. 2012

Antimicrob Agents Chemother

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The distribution of mutants in the Keio collection of Escherichia coli gene knockout mutants that display increased sensitivity to the aminoglycosides kanamycin and neomycin indicates that damaged bases resulting from antibiotic action can lead to cell death. Strains lacking one of a number of glycosylases (e.g., AlkA, YzaB, Ogt, KsgA) or other specific repair proteins (AlkB, PhrB, SmbC) are more sensitive to these antibiotics. Mutants lacking AlkB display the strongest sensitivity among the glycosylase-or direct lesion removaldeficient strains. This perhaps suggests the involvement of ethenoadenine adducts, resulting from reactive oxygen species and lipid peroxidation, since AlkB removes this lesion. Other sensitivities displayed by mutants lacking UvrA, polymerase V (Pol V), or components of double-strand break repair indicate that kanamycin results in damaged base pairs that need to be removed or replicated past in order to avoid double-strand breaks that saturate the cellular repair capacity. Caffeine enhances the sensitivities of these repair-deficient strains to kanamycin and neomycin. The gene knockout mutants that display increased sensitivity to caffeine (dnaQ, holC, holD, and priA knockout mutants) indicate that caffeine blocks DNA replication, ultimately leading to double-strand breaks that require recombinational repair by functions encoded by recA, recB, and recC, among others. Additionally, caffeine partially protects cells of both Escherichia coli and Bacillus anthracis from killing by the widely used fluoroquinolone antibiotic ciprofloxacin.

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“…TDG was previously shown to complement the enzymatic activity of mismatch specific uracil DNA glycosylase (MUG), when expressed in a mug mutant. 36 This complementation of activity by TDG must have a counterpart for balancing the activity of MED1. On the other hand, we found that the MBD could reduce MED1 glycosylase activity, while an inhibitory effect of MBD on G:IU mispairs was not observed when co-incubated with TDG or UDG.…”

Section: Discussionmentioning

confidence: 99%