Abstract
Cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase (UDG), a ubiquitous uracil-excising enzyme found in bacteria and eukaryotes, is one of the enzymes that repair this kind of DNA damage. To date, no UDG-coding gene has been identified in Methanococcus jannaschii, although its entire genome was deciphered. Here, we have identified and characterized a novel UDG from M.jannaschii designated as MjUDG. It efficiently removed uracil from both single- and double-stranded DNA. MjUDG also catalyzes the excision of 8-oxoguanine from DNA. MjUDG has a helix-hairpin-helix motif and a [4Fe-4S]-binding cluster that is considered to be important for the DNA binding and catalytic activity. Although MjUDG shares these features with other structural families such as endonuclease III and mismatch-specific DNA glycosylase (MIG), unique conserved amino acids and substrate specificity distinguish MjUDG from other families. Also, a homologous member of MjUDG was identified in Aquifex aeolicus. We report that MjUDG belongs to a novel UDG family that has not been described to date.
Original language | English |
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Pages (from-to) | 2045-2055 |
Number of pages | 11 |
Journal | Nucleic acids research |
Volume | 31 |
Issue number | 8 |
DOIs | |
Publication status | Published - 2003 Apr 15 |
Bibliographical note
Funding Information:This study was supported by a grant of the Korea Health Research Foundation 21 R&D Project, Ministry of Health and Welfare, Republic of Korea (00-PJ3-PG6-GN01-0001).
All Science Journal Classification (ASJC) codes
- Genetics