Translesional Synthesis Past Acetylaminofluorene-Derived DNA Adducts Catalyzed by Human DNA Polymerase κ and Escherichia coli DNA Polymerase IV†
Identifieur interne : 003456 ( Main/Exploration ); précédent : 003455; suivant : 003457Translesional Synthesis Past Acetylaminofluorene-Derived DNA Adducts Catalyzed by Human DNA Polymerase κ and Escherichia coli DNA Polymerase IV†
Auteurs : Naomi Suzuki [Japon] ; Eiji Ohashi [Japon] ; Ken Hayashi [Japon] ; Haruo Ohmori [Japon] ; Arthur P. Grollman [Japon] ; Shinya Shibutani [Japon, États-Unis]Source :
- Biochemistry [ 0006-2960 ] ; 2001.
Abstract
Human DNA polymerase κ (pol κ) has a sequence significantly homologous with that of Escherichia coli DNA polymerase IV (pol IV). We used a truncated form of human pol κ (pol κΔC) and full-length pol IV to explore the miscoding properties of these enzymes. Oligodeoxynucleotides, modified site-specifically with N-(deoxyguanosin-8-yl)-2-acetylaminofluorene (dG-AAF) and N-(deoxyguanosin-8-yl)-2-aminofluorene (dG-AF), were used as DNA templates in primer extension reactions that included all four dNTPs. Reactions catalyzed by pol κΔC were partially blocked one base prior to dG-AAF or dG-AF, and also opposite both lesions. At higher enzyme concentrations, a significant fraction of primer was extended. Analysis of the fully extended reaction product revealed incorporation of dTMP opposite dG-AAF, accompanied by much smaller amounts of dCMP, dAMP, and dGMP and some one- and two-base deletions. The product terminating 3‘ to the adduct site contained AMP misincorporated opposite dC. On templates containing dG-AF, dAMP, dTMP, and dCMP were incorporated opposite the lesion in approximately equal amounts, together with some one-base and two-base deletions. Steady-state kinetics analysis confirmed the results obtained from primer extension reactions catalyzed by pol κ. In contract, primer extension reactions catalyzed by pol IV were blocked effectively by dG-AAF and dG-AF. At high concentrations of pol IV, full-length products were formed containing primarily one- or two-base deletions with dCMP, the correct base, incorporated opposite dG-AF. The miscoding properties of pol κ observed in this study are consistent with mutational spectra observed when plasmid vectors containing dG-AAF or dG-AF are introduced into simian kidney cells [Shibutani, S., et al. (2001) Biochemistry 40, 3717−3722], supporting a model in which pol κ plays a role in translesion synthesis past acetylaminofluorene-derived lesions in mammalian cells.
Url:
DOI: 10.1021/bi010702g
Affiliations:
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by Human DNA Polymerase κ and <hi rend="italic">Escherichia coli</hi> DNA Polymerase IV<ref type="bib" target="#bi010702gAF2"><hi rend="superscript">†</hi></ref></title><author><name sortKey="Suzuki, Naomi" sort="Suzuki, Naomi" uniqKey="Suzuki N" first="Naomi" last="Suzuki">Naomi Suzuki</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Chemical Biology, Department of Pharmacological Sciences, State University of New York at Stony Brook,Stony Brook, New York 11794-8651, and Institute for Virus Research, Kyoto University, Kyoto 606-8507</wicri:regionArea><wicri:noRegion>Kyoto 606-8507</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Ohashi, Eiji" sort="Ohashi, Eiji" uniqKey="Ohashi E" first="Eiji" last="Ohashi">Eiji Ohashi</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Chemical Biology, Department of Pharmacological Sciences, State University of New York at Stony Brook,Stony Brook, New York 11794-8651, and Institute for Virus Research, Kyoto University, Kyoto 606-8507</wicri:regionArea><wicri:noRegion>Kyoto 606-8507</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Hayashi, Ken" sort="Hayashi, Ken" uniqKey="Hayashi K" first="Ken" last="Hayashi">Ken Hayashi</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Chemical Biology, Department of Pharmacological Sciences, State University of New York at Stony Brook,Stony Brook, New York 11794-8651, and Institute for Virus Research, Kyoto University, Kyoto 606-8507</wicri:regionArea><wicri:noRegion>Kyoto 606-8507</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Ohmori, Haruo" sort="Ohmori, Haruo" uniqKey="Ohmori H" first="Haruo" last="Ohmori">Haruo Ohmori</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Chemical Biology, Department of Pharmacological Sciences, State University of New York at Stony Brook,Stony Brook, New York 11794-8651, and Institute for Virus Research, Kyoto University, Kyoto 606-8507</wicri:regionArea><wicri:noRegion>Kyoto 606-8507</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Grollman, Arthur P" sort="Grollman, Arthur P" uniqKey="Grollman A" first="Arthur P." last="Grollman">Arthur P. 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We used a truncated form of human pol κ (pol κΔC) and full-length pol IV to explore the miscoding properties of these enzymes. Oligodeoxynucleotides, modified site-specifically with N-(deoxyguanosin-8-yl)-2-acetylaminofluorene (dG-AAF) and N-(deoxyguanosin-8-yl)-2-aminofluorene (dG-AF), were used as DNA templates in primer extension reactions that included all four dNTPs. Reactions catalyzed by pol κΔC were partially blocked one base prior to dG-AAF or dG-AF, and also opposite both lesions. At higher enzyme concentrations, a significant fraction of primer was extended. Analysis of the fully extended reaction product revealed incorporation of dTMP opposite dG-AAF, accompanied by much smaller amounts of dCMP, dAMP, and dGMP and some one- and two-base deletions. The product terminating 3‘ to the adduct site contained AMP misincorporated opposite dC. On templates containing dG-AF, dAMP, dTMP, and dCMP were incorporated opposite the lesion in approximately equal amounts, together with some one-base and two-base deletions. Steady-state kinetics analysis confirmed the results obtained from primer extension reactions catalyzed by pol κ. In contract, primer extension reactions catalyzed by pol IV were blocked effectively by dG-AAF and dG-AF. At high concentrations of pol IV, full-length products were formed containing primarily one- or two-base deletions with dCMP, the correct base, incorporated opposite dG-AF. The miscoding properties of pol κ observed in this study are consistent with mutational spectra observed when plasmid vectors containing dG-AAF or dG-AF are introduced into simian kidney cells [Shibutani, S., et al. (2001) Biochemistry 40, 3717−3722], supporting a model in which pol κ plays a role in translesion synthesis past acetylaminofluorene-derived lesions in mammalian cells.</div></front></TEI><affiliations><list><country><li>Japon</li><li>États-Unis</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Suzuki, Naomi" sort="Suzuki, Naomi" uniqKey="Suzuki N" first="Naomi" last="Suzuki">Naomi Suzuki</name></noRegion><name sortKey="Grollman, Arthur P" sort="Grollman, Arthur P" uniqKey="Grollman A" first="Arthur P." last="Grollman">Arthur P. Grollman</name><name sortKey="Hayashi, Ken" sort="Hayashi, Ken" uniqKey="Hayashi K" first="Ken" last="Hayashi">Ken Hayashi</name><name sortKey="Ohashi, Eiji" sort="Ohashi, Eiji" uniqKey="Ohashi E" first="Eiji" last="Ohashi">Eiji Ohashi</name><name sortKey="Ohmori, Haruo" sort="Ohmori, Haruo" uniqKey="Ohmori H" first="Haruo" last="Ohmori">Haruo Ohmori</name><name sortKey="Shibutani, Shinya" sort="Shibutani, Shinya" uniqKey="Shibutani S" first="Shinya" last="Shibutani">Shinya Shibutani</name></country><country name="États-Unis"><noRegion><name sortKey="Shibutani, Shinya" sort="Shibutani, Shinya" uniqKey="Shibutani S" first="Shinya" last="Shibutani">Shinya Shibutani</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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