Binding specificities of the mismatch binding protein, MutS, to oligonucleotides containing modified bases.

K. Negishi, D. Maehara, S. Nakamura, D. Loakes, L. Worth, R. M. Schaaper, K. Seio, M. Sekine, T. Negishi

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Abstract

We have studied the effects of DNA mismatch repair on mutagenesis induced by nucleoside analogs. Among them, the mutagenic action of 3,4-dihydro-6H,8H-pyrimido[4,5-c][1,2]oxazin-7-one 2'-deoxyriboside (dP) showed high susceptibility to the mismatch repair system, while mutagenesis by N4-aminocytidine and N4-hydroxycytidine was only weakly affected. 2-Aminopurine mutagenesis showed intermediate susceptibility. MutS protein specifically bound to an oligonucleotide duplex containing a dP-dG pair, while the dP-dA pair was bound only weakly. The binding to the dP-dG pair was as strong as binding to a dA-dC mismatch. These specific binding properties can explain the effective avoidance of dP-induced mutagenesis by the mismatch repair system. We have also studied the effects of the repair system on mutagenesis induced by methylating and ethylating agents.

Original languageEnglish
Pages (from-to)221-222
Number of pages2
JournalNucleic acids research. Supplement (2001)
Issue number1
DOIs
Publication statusPublished - 2001

ASJC Scopus subject areas

  • Medicine(all)

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    Negishi, K., Maehara, D., Nakamura, S., Loakes, D., Worth, L., Schaaper, R. M., Seio, K., Sekine, M., & Negishi, T. (2001). Binding specificities of the mismatch binding protein, MutS, to oligonucleotides containing modified bases. Nucleic acids research. Supplement (2001), (1), 221-222. https://doi.org/10.1093/nass/1.1.221