Cellular repair mechanism of 5-formyluracil.

A. Masaoka, M. Kobayashi, H. Terato, Y. Ohyama, H. Ide

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

5-Formyluracil (fU) is an oxidative DNA base damage. This damage has been suggested to be mutagenic and but enzymatic repair of the damage is little known. In this study, repair enzymes that recognize fU have been studied. Kinetic analysis of the repair activity of E. coli 3-methyladenine DNA glycosylase II (AlkA) showed that fU was removed by AlkA with the efficiency comparable to 7-methylguanine. We also examined the participation of the methyl-directed mismatch repair system. The affinity of MutS to the fU:G mispair was essentially similar to that of the T:G mispair that was most efficiently recognized by the MutSLH system. These results suggest two distinct repair pathways of fU in E. coli.

Original languageEnglish
Pages (from-to)291-292
Number of pages2
JournalNucleic acids symposium series
Issue number42
DOIs
Publication statusPublished - 1999

ASJC Scopus subject areas

  • Medicine(all)

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