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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Wang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon 97331-7301, USA. haysj@bcc.orst.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon 97331-7301</wicri:regionArea><wicri:noRegion>Oregon 97331-7301</wicri:noRegion></affiliation></author><author><name sortKey="Lawrence, C W" sort="Lawrence, C W" uniqKey="Lawrence C" first="C W" last="Lawrence">C W Lawrence</name></author><author><name sortKey="Li, G M" sort="Li, G M" uniqKey="Li G" first="G M" last="Li">G M Li</name></author><author><name sortKey="Hays, J B" sort="Hays, J B" uniqKey="Hays J" first="J B" last="Hays">J B Hays</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10358035</idno><idno type="pmid">10358035</idno><idno type="doi">10.1074/jbc.274.24.16894</idno><idno type="wicri:Area/PubMed/Corpus">002631</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002631</idno><idno type="wicri:Area/PubMed/Curation">002631</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002631</idno><idno type="wicri:Area/PubMed/Checkpoint">002467</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002467</idno><idno type="wicri:Area/Ncbi/Merge">000018</idno><idno type="wicri:Area/Ncbi/Curation">000018</idno><idno type="wicri:Area/Ncbi/Checkpoint">000018</idno><idno type="wicri:doubleKey">0021-9258:1999:Wang H:specific:binding:of</idno><idno type="wicri:Area/Main/Merge">003826</idno><idno type="wicri:Area/Main/Curation">003782</idno><idno type="wicri:Area/Main/Exploration">003782</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Specific binding of human MSH2.MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil-containing UV light photoproducts opposite mismatched bases.</title><author><name sortKey="Wang, H" sort="Wang, H" uniqKey="Wang H" first="H" last="Wang">H. Wang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon 97331-7301, USA. haysj@bcc.orst.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon 97331-7301</wicri:regionArea><wicri:noRegion>Oregon 97331-7301</wicri:noRegion></affiliation></author><author><name sortKey="Lawrence, C W" sort="Lawrence, C W" uniqKey="Lawrence C" first="C W" last="Lawrence">C W Lawrence</name></author><author><name sortKey="Li, G M" sort="Li, G M" uniqKey="Li G" first="G M" last="Li">G M Li</name></author><author><name sortKey="Hays, J B" sort="Hays, J B" uniqKey="Hays J" first="J B" last="Hays">J B Hays</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Pair Mismatch</term><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></keywords><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></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term><term>Proto-Oncogene Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="radiation effects" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>ADN</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de liaison à l'ADN</term><term>Protéines proto-oncogènes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Pair Mismatch</term><term>DNA Repair</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>Pyrimidine Dimers</term><term>Thymine</term><term>Ultraviolet Rays</term><term>Uracil</term></keywords><keywords scheme="MESH" xml:lang="fr"><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>Rayons ultraviolets</term><term>Réparation de l'ADN</term><term>Thymine</term><term>Uracile</term></keywords></textClass></profileDesc></teiHeader><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></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Hays, J B" sort="Hays, J B" uniqKey="Hays J" first="J B" last="Hays">J B Hays</name><name sortKey="Lawrence, C W" sort="Lawrence, C W" uniqKey="Lawrence C" first="C W" last="Lawrence">C W Lawrence</name><name sortKey="Li, G M" sort="Li, G M" uniqKey="Li G" first="G M" last="Li">G M Li</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Wang, H" sort="Wang, H" uniqKey="Wang H" first="H" last="Wang">H. Wang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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