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Nucleic Acids Symposium Series 2004 48(1):271-272; doi:10.1093/nass/48.1.271
© 2004 by Oxford University Press
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Mutagenesis by damaged deoxyribonucleotides and its prevention by MutT-type hydrolyzing enzymes

Hiroyuki Kamiya, Kazuya Satou, Mika Hori, Emiko Iida, Chieko Ishiguro and Hideyoshi Harashima

Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo 060-0812, Japan

Oxidized deoxyribonucleotides, 2-hydroxydeoxyadenosine 5'-triphosphaie (2-OH-dATP) and 8-hydroxydeoxyguanosine 5'-triphosphate (8-OH-dGTP), were introduced into Escherichia coli strains deficient in DNA polymerase IV (a Y-family DNA polymerase encoded in the dinB gene), and the MutT and Orfl35 proteins to examine their in vivo roles in mutagenesis elicited by 2-OH-dATP and 8-OH-dGTP. 2-OH-dATP elicited mutations less efficiently in the dinB– strain than in the wild type strain, suggesting involvement of DNA polymerase IV in 2-OH-dATP-induced mutations. 8-OH-dGTP and 2-OH-dATP elicited mutations more efficiently in mutT– and orfl35– strains, respectively, than those in their isogenic mutT+ and orfl35+ strains. These results indicate that these proteins play important roles in mutagenesis induced by 2-OH-dATP and 8-OH-dGTP in vivo.


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