Base Excision Repair of Oxidative DNA Damage Activated by XPG Protein
| Autor: | Philip H. Bolton, Stuart G. Clarkson, Paul W. Doetsch, Tomas Lindahl, Daniela Gunz, Matthias Höss, Richard D. Wood, Angelos Constantinou, Arne Klungland |
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| Rok vydání: | 1999 |
| Předmět: |
DNA Repair
DNA repair Molecular Sequence Data Biology AP endonuclease DDB1 Deoxyribonuclease (Pyrimidine Dimer) Humans AP site Cockayne Syndrome Uracil Replication protein A Molecular Biology Binding Sites Endodeoxyribonucleases Base Sequence Escherichia coli Proteins Nuclear Proteins Base excision repair Cell Biology Endonucleases Molecular biology Recombinant Proteins DNA-Binding Proteins Enzyme Activation Oxidative Stress Pyrimidines DNA glycosylase Mutation biology.protein Nucleotide excision repair DNA Damage Transcription Factors |
| Zdroj: | Molecular Cell. 3(1):33-42 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(00)80172-0 |
| Popis: | Oxidized pyrimidines in DNA are removed by a distinct base excision repair pathway initiated by the DNA glycosylase—AP lyase hNth1 in human cells. We have reconstituted this single-residue replacement pathway with recombinant proteins, including the AP endonuclease HAP1/APE, DNA polymerase β, and DNA ligase III-XRCC1 heterodimer. With these proteins, the nucleotide excision repair enzyme XPG serves as a cofactor for the efficient function of hNth1. XPG protein promotes binding of hNth1 to damaged DNA. The stimulation of hNth1 activity is retained in XPG catalytic site mutants inactive in nucleotide excision repair. The data support the model that development of Cockayne syndrome in XP-G patients is related to inefficient excision of endogenous oxidative DNA damage. |
| Databáze: | OpenAIRE |
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