The C-terminal Domain of MutY Glycosylase Determines the 7,8-Dihydro-8-oxo-guanine Specificity and Is Crucial for Mutation Avoidance

Li, Xianghong; Wright, Patrick M.; Lu, A-Lien

doi:10.1074/jbc.275.12.8448

Cited by 56 publications

(95 citation statements)

References 60 publications

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“…hMYH binding to 8oxoG/AP might prevent its action till the abasic site has been fully repaired. Consistent with this model, Li et al (2000) have shown that the tight binding of MUTY to 8oxoG/AP and also to 8oxoG/T and 8oxoG/G has an inhibitory effect on Fpg activity.…”

Section: Discussionsupporting

confidence: 66%

Base excision repair of adenine/8-oxoguanine mispairs by an aphidicolin-sensitive DNA polymerase in human cell extracts

et al. 2002

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Replication of DNA containing 8-oxo-7,8-dihydroguanine (8oxoG) can generate 8oxoG/A base pairs which, if uncorrected, lead to G?T transversions. It is generally accepted that the repair of these promutagenic base pairs in human cells is initiated by the MutY DNA glycosylase homolog (hMYH). Here we provide biochemical evidence that human cell extracts perform base excision repair (BER) on both DNA strands of an 8oxoG/A mismatch. At early repair times the specificity of nucleotide incorporation indicates a preferential insertion of C opposite 8oxoG leading to the formation of 8oxoG/C pairs. This is followed by repair synthesis on the opposite DNA strand that is consistent with hOGG1-mediated correction of 8oxoG/C to G/C. Repair synthesis on either strand is completely inhibited by aphidicolin suggesting that a replicative DNA polymerase is involved in the gap filling. This is the first demonstration that repair of 8oxoG/A base pairs is by two BER events likely mediated by Pold/e. We suggest that the Pold/emediated BER is the general mode of repair when BER lesions are formed at replication forks.

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Section: Discussionsupporting

confidence: 66%

Base excision repair of adenine/8-oxoguanine mispairs by an aphidicolin-sensitive DNA polymerase in human cell extracts

et al. 2002

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“…OGG1 is able to remove 8-oxoG from T/8-oxoG and G/8-oxoG efficiently in vitro (30,31,38). Our laboratory has data to indicate that MutY protein can block and regulate MutM activity (2). Similar to the E.coli MutY/MutM interaction, MYH binding to T/8-oxoG and G/8-oxoG may inhibit OGG1 activity with these substrates.…”

Section: Discussionmentioning

confidence: 73%

“…Over a short reaction period the rate of cleavage of calf mtMYH was much faster for the A/8-oxoG mismatch than other substrates. This substrate reactivity is similar to that of E.coli MutY (2,57,58). In view of the fact that mitochondrial OGG1-like protein will cleave 8-oxoG-containing mismatches and not mismatches paired with G, it is of biological importance that mtMYH binds tightly to A/8-oxoG mismatches but not A/G or A/C mismatches.…”

Section: Discussionmentioning

confidence: 76%

“…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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“…The N-terminal domain of E. coli MutY has the catalytic activity (36 -40); however, the C-terminal domain is important for GO recognition (36,37,40,41). The PCNA binding motifs located at the Cterminal ends of eukaryotic MYH are not conserved in bacterial MutY proteins.…”

Section: The Interactions Between Myh and Pcna Proteins From Both S mentioning

confidence: 99%

Functional Interaction of MutY Homolog with Proliferating Cell Nuclear Antigen in Fission Yeast, Schizosaccharomyces pombe

Chang

2002

Journal of Biological Chemistry

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The MutY homolog (MYH) is responsible for removing adenines misincorporated on a template DNA strand containing G or 7,8-dihydro-8-oxoguanine (8-oxoG) and thus preventing G:C to T:A mutations. Human MYH has been shown to interact physically with human proliferating cell nuclear antigen (hPCNA). Here, we report that a similar interaction between SpMYH and SpPCNA occurs in the fission yeast Schizosaccharomyces pombe. Binding of SpMYH to

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The C-terminal Domain of MutY Glycosylase Determines the 7,8-Dihydro-8-oxo-guanine Specificity and Is Crucial for Mutation Avoidance

Abstract: Escherichia coli

Cited by 56 publications

References 60 publications

Base excision repair of adenine/8-oxoguanine mispairs by an aphidicolin-sensitive DNA polymerase in human cell extracts

Base excision repair of adenine/8-oxoguanine mispairs by an aphidicolin-sensitive DNA polymerase in human cell extracts

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

Functional Interaction of MutY Homolog with Proliferating Cell Nuclear Antigen in Fission Yeast, Schizosaccharomyces pombe

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