Characterization of Escherichia coli Endonuclease VIII

Jiang, Dongyan; Hatahet, Zafer; Melamede, Robert J.; Kow, Yoke W.; Wallace, Susan S.

doi:10.1074/jbc.272.51.32230

Cited by 155 publications

(126 citation statements)

References 63 publications

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“…EndoVIII has been purified and characterized [193] and its gene cloned [194]. The purified enzyme has a molecular mass of 28-30 kDa, and displays β-lyase activity as well as DNA glycosylase activity against thymine glycol and dihydrothymine.…”

Section: Endoviii and Endoixmentioning

confidence: 99%

DNA glycosylases in the base excision repair of DNA

Krokan

Standal

Slupphaug

1997

Biochemical Journal

763

566

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A wide range of cytotoxic and mutagenic DNA bases are removed by different DNA glycosylases, which initiate the base excision repair pathway. DNA glycosylases cleave the Nglycosylic bond between the target base and deoxyribose, thus releasing a free base and leaving an apurinic\apyrimidinic (AP) site. In addition, several DNA glycosylases are bifunctional, since they also display a lyase activity that cleaves the phosphodiester backbone 3h to the AP site generated by the glycosylase activity. Structural data and sequence comparisons have identified common features among many of the DNA glycosylases. Their active sites have a structure that can only bind extrahelical target bases, as observed in the crystal structure of human uracil-DNA glycosylase in a complex with double-stranded DNA. Nucleotide flipping is apparently actively facilitated by the enzyme. With bacteriophage T4 endonuclease V, a pyrimidine-

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Section: Endoviii and Endoixmentioning

confidence: 99%

DNA glycosylases in the base excision repair of DNA

Krokan

Standal

Slupphaug

1997

Biochemical Journal

763

566

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“…A characteristic feature of Fpg/Nei family members is their ability to remove the 5′-dRP moiety generated from incision at abasic sites by human AP endonuclease (APEX) [15,29]. To demonstrate this activity in the mimivirus homologs, a 5′dRP-containing 22-mer substrate was incubated with human NEIL1, MvNei1 and MvNei2.…”

Section: Drp Lyase Activity Of Mvnei1 and Mvnei2mentioning

confidence: 99%

“…Instead, 8-oxoguanine DNA glycosylase (Ogg), a functional homolog of E. coli Fpg is the primary DNA glycosylase that removes 8-oxoguanine in eukaryotes and in archaea. In contrast, endonuclease VIII (Nei) is less commonly found in bacteria and in eukaryotes and until recently, the only Nei protein characterized was endonuclease VIII from E. coli [15]. The first eukaryotic homologs of E. coli Nei designated NEIL1, NEIL2 and NEIL3 (Nei-Like) were recently identified in humans and NEIL1 and NEIL2 extensively characterized [16][17][18][19][20].…”

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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“…Fpg and Nei also share common structural motifs, including helix-two-turns-helix (H2TH) and antiparallel ␤-hairpin zinc finger motifs (6,12). A comparison of EcoNei covalently complexed to DNA (20) with the Fpg structures (21)(22)(23)(24) revealed that their overall folds are very similar; however, their substrate preferences are markedly different: EcoFpg prefers 8-oxoguanine and oxidized purines (25,26), whereas EcoNei recognizes oxidized pyrimidines (19,(27)(28)(29).…”

mentioning

confidence: 99%

“…Catalysis by both E. coli Nei (EcoNei) and Fpg (EcoFpg) is by means of the N-terminal proline, which forms a Schiff base with the oxidized lesion (13)(14)(15). Both EcoNei and EcoFpg are trifunctional enzymes containing glycosylase, ␤,␦ lyase, and 5Ј phosphodiesterase activities (16)(17)(18)(19). Fpg and Nei also share common structural motifs, including helix-two-turns-helix (H2TH) and antiparallel ␤-hairpin zinc finger motifs (6,12).…”

mentioning

confidence: 99%

The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity

Doublié

Bandaru

Bond

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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134

194

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In prokaryotes, two DNA glycosylases recognize and excise oxidized pyrimidines: endonuclease III (Nth) and endonuclease VIII (Nei). The oxidized purine 8-oxoguanine, on the other hand, is recognized by Fpg (also known as MutM), a glycosylase that belongs to the same family as Nei. The recent availability of the human genome sequence allowed the identification of three human homologs of Escherichia coli Nei. We report here the crystal structure of a human Nei-like (NEIL) enzyme, NEIL1. The structure of NEIL1 exhibits the same overall fold as E. coli Nei, albeit with an unexpected twist. Sequence alignments had predicted that NEIL1 would lack a zinc finger, and it was therefore expected to use a different DNA-binding motif instead. Our structure revealed that, to the contrary, NEIL1 contains a structural motif composed of two antiparallel ␤-strands that mimics the antiparallel ␤-hairpin zinc finger found in other Fpg͞Nei family members but lacks the loops that harbor the zinc-binding residues and, therefore, does not coordinate zinc. This ''zincless finger'' appears to be required for NEIL1 activity, because mutating a very highly conserved arginine within this motif greatly reduces the glycosylase activity of the enzyme.

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Characterization of Escherichia coli Endonuclease VIII

Cited by 155 publications

References 63 publications

DNA glycosylases in the base excision repair of DNA

DNA glycosylases in the base excision repair of DNA

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

The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity

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