DNA Determinants and Substrate Specificities of Escherichia coli MutY

Lu, A-Lien; Tsai-Wu, Jyy-Jih; Cillo, Jason

doi:10.1074/jbc.270.40.23582

Cited by 102 publications

(140 citation statements)

References 40 publications

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“…Similar to MutY and all the characterized eukaryotic MutY homologs (4,23,25,26,28,29,53), calf mtMYH exhibits binding and glycosylase activities towards mismatches containing A/8-oxoG and like E.coli MutY (4), S.pombe MYH (53) and partially purified calf nuclear MYH (23), also has good adenine glycosylase activity with A/Gcontaining DNA. However, A/G glycosylase activity is not detected with hMYH expressed by an in vitro transcription/ translation system (28) and is very weak from E.coli expressed hMYH (26,29).…”

Section: Discussionmentioning

confidence: 99%

“…If mtMYH has an AP lyase activity and uses the similar reaction mechanism as MutY does (54), an imino (Shiff base) intermediate should be reduced by NaBH 4 to form a covalent protein-DNA complex. To test this, trapping reactions to detect covalently bound enzyme-DNA complexes were performed with mtMYH and A/8-oxoG-containing DNA in the presence of different concentrations of NaBH 4 . A very weak mtMYH-DNA covalent complex was detected in the presence of (10-50 mM) NaBH 4 (data not shown).…”

Section: Further Characterization Of Calf Mtmyhmentioning

confidence: 99%

“…Base excision repair by Escherichia coli MutY glycosylase corrects the base-base mismatches A/G and A/C as well as adenine and guanine paired with 7,8-dihydro-8-oxo-deoxyguanine (8-oxoG) that arise through DNA replication errors and DNA recombination (1)(2)(3)(4)(5)(6)(7)(8)(9). Together with MutM and MutT, the MutY protein helps to protect the bacteria from the mutagenic effects of 8-oxoG (10,11), the most stable product known caused by oxidative damage to DNA (12,13).…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of a mammalian homolog of Escherichia coli MutY mismatch repair protein from calf liver mitochondria

Parker

2000

Nucleic Acids Research

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A protein homologous to the Escherichia coli MutY glycosylase, referred to as mtMYH, has been purified from calf liver mitochondria. SDS-polyacrylamide gel electrophoresis, western blot analysis as well as gel filtration chromatography predicted the molecular mass of the purified calf mtMYH to be 35-40 kDa. Gel mobility shift analysis showed that the purified mtMYH formed specific binding complexes with A/8-oxoG, G/8-oxoG and T/8-oxoG, weakly with C/8-oxoG, but not with A/G and A/C mismatches. The purified mtMYH exhibited DNA glycosylase activity removing adenine mispaired with G, C or 8-oxoG and weakly removing guanine mispaired with 8-oxoG. The mtMYH glycosylase activity was insensitive to high concentrations of NaCl and EDTA. The purified mtMYH cross-reacted with antibodies against both intact MutY and a peptide of human MutY homolog (hMYH). DNA glycosylase activity of mtMYH was inhibited by anti-MutY antibodies but not by antihMYH peptide antibodies. Together with the previously described mitochondrial MutT homolog (MTH1) and 8-oxoG glycosylase (OGG1, a functional MutM homolog), mtMYH can protect mitochondrial DNA from the mutagenic effects of 8-oxoG.

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Section: Discussionmentioning

confidence: 99%

Section: Further Characterization Of Calf Mtmyhmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of a mammalian homolog of Escherichia coli MutY mismatch repair protein from calf liver mitochondria

Parker

2000

Nucleic Acids Research

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“…Thus MutY apparently serves an important function in protection against oxidative damage by removing adenine mispaired to 8-oxoG after replication. The substrate specificity of MutY has been extensively studied, but it is not clear whether A\G or A\8-oxoG is the preferred substrate [97,98]. As described below, several glycosylases take part in the repair of oxidized bases.…”

Section: G/t(u)-mismatch Dna Glycosylasesmentioning

confidence: 99%

DNA glycosylases in the base excision repair of DNA

Krokan

Standal

Slupphaug

1997

Biochemical Journal

771

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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“…MutY, structurally similar to Endo III [18][19][20][21], is another BER glycosylase that contains a [4Fe-4S] cluster [20]. However, MutY instead removes adenine from 8-oxo-guanine:adenine mispairs [22][23][24][25][26][27][28][29][30][31][32][33][34].…”

Section: Introductionmentioning

confidence: 99%

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Boal

Yavin

Barton

2007

Journal of Inorganic Biochemistry

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The [4Fe-4S] cluster is ubiquitous to a class of base excision repair enzymes, in organisms ranging from bacteria to man, and was first considered as a structural element, owing to its redox stability under physiological conditions. When studied bound to DNA, two of these repair proteins (MutY and Endonuclease III from Escherichia coli) display DNA-dependent reversible electron transfer with characteristics typical of high potential iron proteins. These results have inspired a reexamination of the role of the [4Fe-4S] cluster in this class of enzymes. Might the [4Fe-4S] cluster be used as a redox cofactor to search for damaged sites using DNA-mediated charge transport, a process well known to be highly sensitive to lesions and mismatched bases? Described here are experiments demonstrating the utility of DNA-mediated charge transport in characterizing these DNA-binding metalloproteins, as well as efforts to elucidate this new function for DNA as an electronic signaling medium among the proteins.

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DNA Determinants and Substrate Specificities of Escherichia coli MutY

Cited by 102 publications

References 40 publications

Purification and characterization of a mammalian homolog of Escherichia coli MutY mismatch repair protein from calf liver mitochondria

Purification and characterization of a mammalian homolog of Escherichia coli MutY mismatch repair protein from calf liver mitochondria

DNA glycosylases in the base excision repair of DNA

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

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