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Nucleic Acids Research, 2003, Vol. 31, No. 8 2045-2055
© 2003 Oxford University Press

A novel uracil-DNA glycosylase family related to the helix–hairpin–helix DNA glycosylase superfamily

Ji Hyung Chung1,2,3, Eun Kyoung Im2,3, Hyun-Young Park1,2,3, Jun Hye Kwon2,4, Seahyoung Lee2, Jaewon Oh2, Ki-Chul Hwang2,3, Jong Ho Lee1,2,3 and Yangsoo Jang1,2,3,4

1 Yonsei Research Institute of Aging Science, 2 Cardiovascular Research Institute, 3 Cardiovascular Genome Center and 4 Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Yonsei University, Seoul, 120-752, Korea

The authors wish it to be known that, in their opinion, the first two authors should be considered as joint First Authors

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.


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