Specific binding of human MSH2.MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil-containing UV light photoproducts opposite mismatched bases.
Identifieur interne : 003782 ( Main/Exploration ); précédent : 003781; suivant : 003783Specific binding of human MSH2.MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil-containing UV light photoproducts opposite mismatched bases.
Auteurs : H. Wang [États-Unis] ; C W Lawrence ; G M Li ; J B HaysSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- ADN (effets des radiations), Dimères de pyrimidine, Dimérisation, Humains, Liaison aux protéines, Modèles génétiques, Mutagenèse, Mésappariement de bases, Protéine-2 homologue de MutS, Protéines de liaison à l'ADN (métabolisme), Protéines proto-oncogènes (métabolisme), Rayons ultraviolets, Réparation de l'ADN, Thymine, Uracile.
- MESH :
- effets des radiations : ADN.
- métabolisme : Protéines de liaison à l'ADN, Protéines proto-oncogènes.
- Dimères de pyrimidine, Dimérisation, Humains, Liaison aux protéines, Modèles génétiques, Mutagenèse, Mésappariement de bases, Protéine-2 homologue de MutS, Rayons ultraviolets, Réparation de l'ADN, Thymine, Uracile.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : DNA-Binding Proteins, Proto-Oncogene Proteins.
- chemical , radiation effects : DNA.
- Base Pair Mismatch, DNA Repair, Dimerization, Humans, Models, Genetic, MutS Homolog 2 Protein, Mutagenesis, Protein Binding, Pyrimidine Dimers, Thymine, Ultraviolet Rays, Uracil.
Abstract
Previous studies have demonstrated recognition of DNA-containing UV light photoproducts by bacterial (Feng, W.-Y., Lee, E., and Hays, J. B. (1991) Genetics 129, 1007-1020) and human (Mu, D., Tursun, M., Duckett, D. R., Drummond, J. T., Modrich, P., and Sancar, A. (1997) Mol. Cell. Biol. 17, 760-769) long-patch mismatch-repair systems. Mismatch repair directed specifically against incorrect bases inserted during semi-conservative DNA replication might efficiently antagonize UV mutagenesis. To test this hypothesis, DNA 51-mers containing site-specific T-T cis-syn-cyclobutane pyrimidine-dimers or T-T pyrimidine-(6-4')pyrimidinone photoproducts, with all four possible bases opposite the respective 3'-thymines in the photoproducts, were analyzed for the ability to compete with radiolabeled (T/G)-mismatched DNA for binding by highly purified human MSH2.MSH6 heterodimer protein (hMutSalpha). Both (cyclobutane-dimer)/AG and ((6-4)photoproduct)/AG mismatches competed about as well as non-photoproduct T/T mismatches. The two respective pairs of photoproduct/(A(T or C)) mismatches also showed higher hMutSalpha affinity than photoproduct/AA "matches"; the apparent affinity of hMutSalpha for the ((6-4)photoproduct)/AA-"matched" substrate was actually less than that for TT/AA homoduplexes. Surprisingly, although hMutSalpha affinities for both non-photoproduct UU/GG double mismatches and for (uracil-cyclobutane-dimer)/AG single mismatches were high, affinity for the (uracil-cyclobutane-dimer)/GG mismatch was quite low. Equilibrium binding of hMutSalpha to DNA containing (photoproduct/base) mismatches and to (T/G)-mismatched DNA was reduced similarly by ATP (in the absence of magnesium).
DOI: 10.1074/jbc.274.24.16894
PubMed: 10358035
Affiliations:
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Le document en format XML
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<term>DNA (radiation effects)</term>
<term>DNA Repair</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Dimerization</term>
<term>Humans</term>
<term>Models, Genetic</term>
<term>MutS Homolog 2 Protein</term>
<term>Mutagenesis</term>
<term>Protein Binding</term>
<term>Proto-Oncogene Proteins (metabolism)</term>
<term>Pyrimidine Dimers</term>
<term>Thymine</term>
<term>Ultraviolet Rays</term>
<term>Uracil</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN (effets des radiations)</term>
<term>Dimères de pyrimidine</term>
<term>Dimérisation</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Modèles génétiques</term>
<term>Mutagenèse</term>
<term>Mésappariement de bases</term>
<term>Protéine-2 homologue de MutS</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Protéines proto-oncogènes (métabolisme)</term>
<term>Rayons ultraviolets</term>
<term>Réparation de l'ADN</term>
<term>Thymine</term>
<term>Uracile</term>
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<term>MutS Homolog 2 Protein</term>
<term>Mutagenesis</term>
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<term>Liaison aux protéines</term>
<term>Modèles génétiques</term>
<term>Mutagenèse</term>
<term>Mésappariement de bases</term>
<term>Protéine-2 homologue de MutS</term>
<term>Rayons ultraviolets</term>
<term>Réparation de l'ADN</term>
<term>Thymine</term>
<term>Uracile</term>
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<front><div type="abstract" xml:lang="en">Previous studies have demonstrated recognition of DNA-containing UV light photoproducts by bacterial (Feng, W.-Y., Lee, E., and Hays, J. B. (1991) Genetics 129, 1007-1020) and human (Mu, D., Tursun, M., Duckett, D. R., Drummond, J. T., Modrich, P., and Sancar, A. (1997) Mol. Cell. Biol. 17, 760-769) long-patch mismatch-repair systems. Mismatch repair directed specifically against incorrect bases inserted during semi-conservative DNA replication might efficiently antagonize UV mutagenesis. To test this hypothesis, DNA 51-mers containing site-specific T-T cis-syn-cyclobutane pyrimidine-dimers or T-T pyrimidine-(6-4')pyrimidinone photoproducts, with all four possible bases opposite the respective 3'-thymines in the photoproducts, were analyzed for the ability to compete with radiolabeled (T/G)-mismatched DNA for binding by highly purified human MSH2.MSH6 heterodimer protein (hMutSalpha). Both (cyclobutane-dimer)/AG and ((6-4)photoproduct)/AG mismatches competed about as well as non-photoproduct T/T mismatches. The two respective pairs of photoproduct/(A(T or C)) mismatches also showed higher hMutSalpha affinity than photoproduct/AA "matches"; the apparent affinity of hMutSalpha for the ((6-4)photoproduct)/AA-"matched" substrate was actually less than that for TT/AA homoduplexes. Surprisingly, although hMutSalpha affinities for both non-photoproduct UU/GG double mismatches and for (uracil-cyclobutane-dimer)/AG single mismatches were high, affinity for the (uracil-cyclobutane-dimer)/GG mismatch was quite low. Equilibrium binding of hMutSalpha to DNA containing (photoproduct/base) mismatches and to (T/G)-mismatched DNA was reduced similarly by ATP (in the absence of magnesium).</div>
</front>
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