Mechanism-Based DNA−Protein Cross-Linking of MutY via Oxidation of 8-Oxoguanosine

Hickerson, Robyn P.; Chepanoske, Cindy Lou; Williams, S. D.; David, Sheila S.; Burrows, Cynthia J.

doi:10.1021/ja9923484

Cited by 51 publications

(58 citation statements)

References 22 publications

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“…Prompted by earlier investigations of metalcatalyzed guanine oxidation, studies in our laboratory have recently focused on the oneelectron pathway of OG oxidation (17)(18)(19)(20)(21) Figure 3 (21). The formation of Gh is further complicated by its isomerization to iminoallantoin (Ia) (23).…”

Section: Characterization Of New Oxidized Lesionsmentioning

confidence: 99%

Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals.

Burrows

Muller

Kornyushyna

et al. 2002

Environ Health Perspect

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In vitro work in this laboratory has identified new DNA lesions resulting from further oxidation of a common biomarker of oxidative damage, 8-oxo-7,8-dihydroguanine (OG). The major product of oxidation of OG in a nucleoside, nucleotide, or single-stranded oligodeoxynucleotide using metal ions that act as one-electron oxidants is the new nucleoside derivative spiroiminodihydantoin (Sp). In duplex DNA an equilibrating mixture of two isomeric products, guanidinohydantoin (Gh) and iminoallantoin (Ia), is produced. These products are also formed by the overall four-electron oxidation of guanosine by photochemical processes involving O 2 . DNA template strands containing either Sp or Gh/Ia generally acted as a block to DNA synthesis with the Klenow exo -fragment of pol I. However, when nucleotide insertion did occur opposite the lesions, only 2´-deoxyadenosine 5-triphosphate and 2´-deoxyguanine 5-triphosphate were used for primer extension. The Escherichia coli DNA repair enzyme Fpg was able to remove the Sp and Gh/Ia lesions from duplex DNA substrates, although the efficiency was depended on the base opposite the lesion.

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Section: Characterization Of New Oxidized Lesionsmentioning

confidence: 99%

Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals.

Burrows

Muller

Kornyushyna

et al. 2002

Environ Health Perspect

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“…On the other hand formamidopyrimidine DNA glycosylase (EcoFpg) recognizes mainly 8-oxoguanine (8-oxoG) and formamidopyrimidine derivatives of 'A' (FapyA) and 'G' (FapyG) [4]. More recently it has been shown that due to its low redox potential, 8-oxoG can undergo further oxidation to yield ring-opened products, spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) [5][6][7][8]. These lesions are highly mutagenic and result in G→T and G→C transversion mutations [9,10].…”

Section: Introductionmentioning

confidence: 99%

Human endonuclease VIII-like (NEIL) proteins in the giant DNA Mimivirus

et al. 2007

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Endonuclease VIII (Nei), which recognizes and repairs oxidized pyrimidines in the Base Excision Repair (BER) pathway, is sparsely distributed among both the prokaryotes and eukaryotes. Recently, we and others identified three homologs of E. coli endonuclease VIII-like (NEIL) proteins in humans. Here, we report identification of human NEIL homologs in Mimivirus, a giant DNA virus that infects Acanthamoeba. Characterization of the two mimiviral homologs, MvNei1 and MvNei2, showed that they share not only sequence homology but also substrate specificity to the human NEIL proteins, that is, they recognize oxidized pyrimidines in duplex DNA and in bubble substrates and as well show 5′2-deoxyribose-5-phosphate lyase (dRP lyase) activity. However, unlike MvNei1 and the human NEIL proteins, MvNei2 preferentially cleaves oxidized pyrimidines in single stranded DNA forming products with a different end chemistry. Interestingly, opposite base specificity of MvNei1 resembles human NEIL proteins for pyrimidine base damages whereas it resembles E. coli formamidopyrimidine DNA glycosylase (Fpg) for guanidinohydantoin (Gh), an oxidation product of 8-oxoguanine. Finally, a conserved arginine residue in the "zincless finger" motif, previously identified in human NEIL1, is required for the DNA glycosylase activity of MvNeil. Thus, Mimivirus represents the first example of a virus to carry oxidative DNA glycosylases with substrate specificities that resemble human NEIL proteins. Based on the sequence homology to the human NEIL homologs and novel bacterial NEIL homologs identified here, we predict that Mimivirus may have acquired the DNA glycosylases through the host-mediated lateral transfer from either a bacterium or from vertebrates.

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“…A novel method of oxidatively inducing DNA-protein cross-links has been reported using 2′-deoxy-8-oxo-7,8-dihydroguanosine (OG)-substituted DNA [12,13]. In the presence of Na 2 IrCl 6 , OG is readily oxidized to create an electron-deficient center highly susceptible to attack by a nearby nucleophilic protein side chain [12,14].…”

Section: Introductionmentioning

confidence: 99%

“…In the presence of Na 2 IrCl 6 , OG is readily oxidized to create an electron-deficient center highly susceptible to attack by a nearby nucleophilic protein side chain [12,14]. Since cross-link formation requires that two functional groups be within hydrogen bonding distance, interactions can be mapped with high precision using this approach.…”

Section: Introductionmentioning

confidence: 99%

Functional guanine–arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis

Burke

Musier‐Forsyth

2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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SummaryAminoacyl-tRNA synthetases catalyze the attachment of specific amino acids to their cognate tRNAs. Specific aminoacylation is dictated by a set of recognition elements that mark tRNA molecules as substrates for particular synthetases. Escherichia coli prolyl-tRNA synthetase (ProRS) has previously been shown to recognize specific bases of tRNA Pro in both the anticodon domain, which mediate initial complex formation, and in the acceptor stem, which is proximal to the site of catalysis. In this work, we unambiguously define the molecular interaction between E. coli ProRS and the acceptor stem of cognate tRNA Pro . Oxidative cross-linking studies using 2′-deoxy-8-oxo-7,8-dihydroguanosine-containing proline tRNAs identify a direct interaction between a critical arginine residue (R144) in the active site of E. coli ProRS and the G72 residue in the acceptor stem of tRNA Pro . Assays conducted with motif 2 loop variants and tRNA mutants wherein specific atomic groups of G72 were deleted, are consistent with a functionally important hydrogen bonding network between R144 and the major groove of G72. These results taken together with previous studies suggest that breaking this key contact uncouples the allosteric interaction between the anticodon domain and the aminoacylation active site, providing new insights into the communication network that governs the synthetase-tRNA interaction.

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Mechanism-Based DNA−Protein Cross-Linking of MutY via Oxidation of 8-Oxoguanosine

Cited by 51 publications

References 22 publications

Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals.

Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals.

Human endonuclease VIII-like (NEIL) proteins in the giant DNA Mimivirus

Functional guanine–arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis

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