PMID:16201966
| Citation |
Lu, AL, Lee, CY, Li, L and Li, X (2006) Physical and functional interactions between Escherichia coli MutY and endonuclease VIII. Biochem. J. 393:381-7 |
|---|---|
| Abstract |
Both GO (7,8-dihydro-8-oxoguanine) and hoU (5-hydroxyuracil) are highly mutagenic because DNA polymerase frequently misincorporates adenine opposite these damaged bases. In Escherichia coli, MutY DNA glycosylase can remove misincorporated adenine opposite G or GO on the template strand during DNA replication. MutY remains bound to the product that contains an AP (apurinic/apyrimidinic) site. Endo VIII (endonuclease VIII) can remove oxidized pyrimidine and weakly remove GO by its DNA glycosylase and beta/delta-elimination activities. In the present paper, we demonstrate that Endo VIII can promote MutY dissociation from AP/G, but not from AP/GO, and can promote beta/delta-elimination on the products of MutY. MutY interacts physically with Endo VIII through its C-terminal domain. MutY has a moderate affinity for DNA containing a hoU/A mismatch, which is a substrate of Endo VIII. MutY competes with Endo VIII and inhibits Endo VIII activity on DNA that contains a hoU/A mismatch. Moreover, MutY has a weak adenine glycosylase activity on hoU/A mismatches. These results suggest that MutY may have some role in reducing the mutagenic effects of hoU. |
| Links |
PubMed PMC1383697 Online version:10.1042/BJ20051133 |
| Keywords |
DNA Glycosylases/metabolism; DNA, Bacterial/metabolism; Deoxyribonuclease (Pyrimidine Dimer)/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Guanine/analogs & derivatives; Guanine/metabolism; Protein Binding; Protein Conformation; Uracil/analogs & derivatives; Uracil/metabolism |
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