Damage specificity of human DNA glycosylases for oxidative pyrimidine lesions.

Atsushi Katafuchi, Mayumi Matsubara, Hiroaki Terato, Shigenori Iwai, Fumio Hanaoka, Hiroshi Ide

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Abstract

Endo III and Endo VIII are major E. coli DNA glycosylases that remove oxidatively damaged pyrimidine bases. In the present study, we have compared the damage specificity of human homologues of Endo III (hNTHl) and Endo VIII (hNEIL1 and hNEIL2) to elucidate the repair role in cells. hNTH1 and hNEIL1 recognized a similar spectra of bases lesions, but the preference of damage including the stereoisomers of thymine glycol was significantly different between hNTH1 and hNEIL1. hNEIL2 exhibited a strong AP lyase activity but the N-glycosylase activity for the tested oxidative base lesions was marginal.

Original languageEnglish
Pages (from-to)175-176
Number of pages2
JournalNucleic acids symposium series (2004)
Issue number48
Publication statusPublished - 2004
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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    Katafuchi, A., Matsubara, M., Terato, H., Iwai, S., Hanaoka, F., & Ide, H. (2004). Damage specificity of human DNA glycosylases for oxidative pyrimidine lesions. Nucleic acids symposium series (2004), (48), 175-176.