PMID:10780494

Citation	*Masaoka, A, Kobayashi, M, Terato, H, Ohyama, Y and Ide, H' (1999) Cellular repair mechanism of 5-formyluracil.* Nucleic Acids Symp. Ser. '**:291-2
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.
Links	PubMed
Keywords	Base Pair Mismatch; Carbon-Oxygen Lyases/metabolism; Cloning, Molecular; DNA Damage; DNA Glycosylases; DNA Repair; DNA-(Apurinic or Apyrimidinic Site) Lyase; Deoxyribonuclease IV (Phage T4-Induced); Escherichia coli/enzymology; Escherichia coli Proteins; N-Glycosyl Hydrolases/metabolism; Recombinant Proteins/metabolism; Uracil/analogs & derivatives
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