Deoxyxanthosine in DNA is repaired by Escherichia coli endonuclease V

He, Bin; Qing, Hong; Kow, Yoke W.

doi:10.1016/s0921-8777(99)00063-4

Cited by 62 publications

(70 citation statements)

References 23 publications

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“…The rdgB mutants experience increased levels of double-strand breaks in their chromosome, implicating the RdgB protein in avoidance of chromosomal fragmentation (Bradshaw and Kuzminov 2003;. Both the chromosomal fragmentation and the synthetic lethality of rdgB rec mutants are suppressed by inactivation of Endo V (Bradshaw and Kuzminov 2003), which nicks DNA near hypoxanthine and xanthine residues (Yao et al 1994;Yao and Kow 1995;He et al 2000). Moreover, DNA in rdgB mutants accumulates EndoV-recognized modifications (Bradshaw and Kuzminov 2003).…”

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confidence: 99%

Chromosomal Fragmentation Is the Major Consequence of the rdgB Defect in Escherichia coli

Lukas

Kuzminov

2006

Genetics

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confidence: 99%

Chromosomal Fragmentation Is the Major Consequence of the rdgB Defect in Escherichia coli

Lukas

Kuzminov

2006

Genetics

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“…E. coli endo V has been shown to have deoxyxanthosine endonuclease activity (19,20). Human alkyladenine glycosylase (AAG, also called MPG for methylpurine DNA glycosylase) has also been shown to have xanthine DNA glycosylase activity 2 (9).…”

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confidence: 99%

Oxanine DNA Glycosylase Activity from Mammalian Alkyladenine Glycosylase

Hitchcock

Dong

Connor

et al. 2004

Journal of Biological Chemistry

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Oxanine (Oxa) is a deaminated base lesion derived from guanine in which the N 1 -nitrogen is substituted by oxygen. This work reports the mutagenicity of oxanine as well as oxanine DNA glycosylase (ODG) activities in mammalian systems. Using human DNA polymerase ␤, deoxyoxanosine triphosphate is only incorporated opposite cytosine (Cyt). When an oxanine base is in a DNA template, Cyt is efficiently incorporated opposite the template oxanine; however, adenine and thymine are also incorporated opposite Oxa with an efficiency ϳ80% of a Cyt/Oxa (C/O) base pair. Guanine is incorporated opposite Oxa with the least efficiency, 16% compared with cytosine. ODG activity was detected in several mammalian cell extracts. Among the known human DNA glycosylases tested, human alkyladenine glycosylase (AAG) shows ODG activity, whereas hOGG1, hNEIL1, or hNEIL2 did not. ODG activity was detected in spleen cell extracts of wild type age-matched mice, but little activity was observed in that of Aag knock-out mice, confirming that the ODG activity is intrinsic to AAG. Human AAG can excise Oxa from all four Oxa-containing double-stranded base pairs, Cyt/Oxa, Thy/Oxa, Ade/Oxa, and Gua/Oxa, with no preference to base pairing. Surprisingly, AAG can remove Oxa from single-stranded Oxacontaining DNA as well. Indeed, AAG can also remove 1,N 6 -ethenoadenine from single-stranded DNA. This study extends the deaminated base glycosylase activities of AAG to oxanine; thus, AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine.

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“…We are interested in achieving a comprehensive understanding of xanthine DNA repair in E. coli. Previous studies show that AlkA, endo VIII, and endo V in E. coli possess xanthine repair activities (11,12,16). Using an E. coli triple mutant strain (nfi nei alkA), we detected xanthine DNA glycosylase (XDG) activity in whole cell protein extracts.…”

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confidence: 89%

“…Previous investigations using purified enzymes revealed that two glycosylases (AlkA and endo VIII) and endo V in E. coli possess xanthine DNA glycosylase activity or deoxyxanthosine endonuclease activity (11,12,16). However, XDG activities from the two glycosylases, particularly the latter, are quite low.…”

Section: Detection Of Xdg Activity In E Coli Cell Extracts-studiesmentioning

confidence: 99%

Identification of Escherichia coli Mismatch-specific Uracil DNA Glycosylase as a Robust Xanthine DNA Glycosylase

Lee

Brice

Wright

et al. 2010

Journal of Biological Chemistry

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The gene for the mismatch-specific uracil DNA glycosylase (MUG) was identified in the Escherichia coli genome as a sequence homolog of the human thymine DNA glycosylase with activity against mismatched uracil base pairs. Examination of cell extracts led us to detect a previously unknown xanthine DNA glycosylase (XDG) activity in E. coli. DNA glycosylase assays with purified enzymes indicated the novel XDG activity is attributable to MUG. Here, we report a biochemical characterization of xanthine DNA glycosylase activity in MUG. The wild type MUG possesses more robust activity against xanthine than uracil and is active against all xanthine-containing DNA (C/X, T/X, G/X, A/X and single-stranded X). Analysis of potentials of mean force indicates that the double-stranded xanthine base pairs have a relatively narrow energetic difference in base flipping, whereas the tendency for uracil base flipping follows the order of C/U > G/U > T/U > A/U. Site-directed mutagenesis performed on conserved motifs revealed that Asn-140 and Ser-23 are important determinants for XDG activity in E. coli MUG. Molecular modeling and molecular dynamics simulations reveal distinct hydrogen-bonding patterns in the active site of E. coli MUG that account for the specificity differences between E. coli MUG and human thymine DNA glycosylase as well as that between the wild type MUG and the Asn-140 and Ser-23 mutants. This study underscores the role of the favorable binding interactions in modulating the specificity of DNA glycosylases.

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Deoxyxanthosine in DNA is repaired by Escherichia coli endonuclease V

Cited by 62 publications

References 23 publications

Chromosomal Fragmentation Is the Major Consequence of the rdgB Defect in Escherichia coli

Chromosomal Fragmentation Is the Major Consequence of the rdgB Defect in Escherichia coli

Oxanine DNA Glycosylase Activity from Mammalian Alkyladenine Glycosylase

Identification of Escherichia coli Mismatch-specific Uracil DNA Glycosylase as a Robust Xanthine DNA Glycosylase

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