8-Oxoguanine DNA Glycosylases: One Lesion, Three Subfamilies
| Autor: | Sylvie Doublié, Zongchao Jia, Frédérick Faucher |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Review
Ligands medicine.disease_cause 01 natural sciences Protein Structure Secondary DNA Glycosylases lcsh:Chemistry chemistry.chemical_compound heterocyclic compounds lcsh:QH301-705.5 Spectroscopy Genetics 0303 health sciences Mutation protein-DNA complex General Medicine Base excision repair computer.file_format Computer Science Applications Protein Binding Guanine DNA repair Molecular Sequence Data Ogg 8-oxoguanine DNA glycosylase Protein-DNA complex Biology 010402 general chemistry base excision repair Catalysis Inorganic Chemistry 03 medical and health sciences Bacterial Proteins medicine Animals Humans Amino Acid Sequence Physical and Theoretical Chemistry crystallography Molecular Biology 030304 developmental biology OGG Organic Chemistry DNA 8-Oxoguanine Protein Structure Tertiary 0104 chemical sciences chemistry lcsh:Biology (General) lcsh:QD1-999 DNA glycosylase 8-oxoguanine Reactive Oxygen Species computer |
| Zdroj: | International Journal of Molecular Sciences, Vol 13, Iss 6, Pp 6711-6729 (2012) International Journal of Molecular Sciences |
| ISSN: | 1422-0067 |
| Popis: | Amongst the four bases that form DNA, guanine is the most susceptible to oxidation, and its oxidation product, 7,8-dihydro-8-oxoguanine (8-oxoG) is the most prevalent base lesion found in DNA. Fortunately, throughout evolution cells have developed repair mechanisms, such as the 8-oxoguanine DNA glycosylases (OGG), which recognize and excise 8-oxoG from DNA thereby preventing the accumulation of deleterious mutations. OGG are divided into three subfamilies, OGG1, OGG2 and AGOG, which are all involved in the base excision repair (BER) pathway. The published structures of OGG1 and AGOG, as well as the recent availability of OGG2 structures in both apo- and liganded forms, provide an excellent opportunity to compare the structural and functional properties of the three OGG subfamilies. Among the observed differences, the three-dimensional fold varies considerably between OGG1 and OGG2 members, as the latter lack the A-domain involved in 8-oxoG binding. In addition, all three OGG subfamilies bind 8-oxoG in a different manner even though the crucial interaction between the enzyme and the protonated N7 of 8-oxoG is conserved. Finally, the three OGG subfamilies differ with respect to DNA binding properties, helix-hairpin-helix motifs, and specificity for the opposite base. |
| Databáze: | OpenAIRE |
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