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PMID:11238902
| Citation |
Unk, I, Haracska, L, Prakash, S and Prakash, L (2001) 3'-phosphodiesterase and 3'-->5' exonuclease activities of yeast Apn2 protein and requirement of these activities for repair of oxidative DNA damage. Mol. Cell. Biol. 21:1656-61 |
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| Abstract |
In Saccharomyces cerevisiae, the AP endonucleases encoded by the APN1 and APN2 genes provide alternate pathways for the removal of abasic sites. Oxidative DNA-damaging agents, such as H(2)O(2), produce DNA strand breaks which contain 3'-phosphate or 3'-phosphoglycolate termini. Such 3' termini are inhibitory to synthesis by DNA polymerases. Here, we show that purified yeast Apn2 protein contains 3'-phosphodiesterase and 3'-->5' exonuclease activities, and mutation of the active-site residue Glu59 to Ala in Apn2 inactivates both these activities. Consistent with these biochemical observations, genetic studies indicate the involvement of APN2 in the repair of H(2)O(2)-induced DNA damage in a pathway alternate to APN1, and the Ala59 mutation inactivates this function of Apn2. From these results, we conclude that the ability of Apn2 to remove 3'-end groups from DNA is paramount for the repair of strand breaks arising from the reaction of DNA with reactive oxygen species. |
| Links |
PubMed PMC86711 Online version:10.1128/MCB.21.5.1656-1661.2001 |
| Keywords |
Alanine/chemistry; Base Sequence; Binding Sites; Carbon-Oxygen Lyases/chemistry; Carbon-Oxygen Lyases/physiology; DNA Damage; DNA Repair; DNA-(Apurinic or Apyrimidinic Site) Lyase; Deoxyribonuclease IV (Phage T4-Induced); Dose-Response Relationship, Drug; Exodeoxyribonuclease V; Exodeoxyribonucleases/metabolism; Glutamic Acid/chemistry; Glutathione Transferase/metabolism; Hydrogen Peroxide/pharmacology; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutation; Nucleotidases/metabolism; Oxygen/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins; Substrate Specificity; Time Factors |
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Significance
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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