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 |
|---|---|
| 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 |
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All Science Journal Classification (ASJC) codes
- Genetics
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A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily. / Chung, Ji Hyung; Im, Eun Kyoung; Park, Hyun Young; Kwon, Jun Hye; Lee, Seahyoung; Oh, Jaewon; Hwang, Ki Chul; Lee, Jong Ho; Jang, Yangsoo.
In: Nucleic acids research, Vol. 31, No. 8, 15.04.2003, p. 2045-2055.Research output: Contribution to journal › Article
TY - JOUR
T1 - A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily
AU - Chung, Ji Hyung
AU - Im, Eun Kyoung
AU - Park, Hyun Young
AU - Kwon, Jun Hye
AU - Lee, Seahyoung
AU - Oh, Jaewon
AU - Hwang, Ki Chul
AU - Lee, Jong Ho
AU - Jang, Yangsoo
PY - 2003/4/15
Y1 - 2003/4/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037799511&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037799511&partnerID=8YFLogxK
U2 - 10.1093/nar/gkg319
DO - 10.1093/nar/gkg319
M3 - Article
C2 - 12682355
AN - SCOPUS:0037799511
VL - 31
SP - 2045
EP - 2055
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 8
ER -