PMID:9360960
| Citation |
Paz-Elizur, T, Barak, Y and Livneh, Z (1997) Anti-mutagenic activity of DNA damage-binding proteins mediated by direct inhibition of translesion replication. J. Biol. Chem. 272:28906-11 |
|---|---|
| Abstract |
DNA lesions that block replication can be bypassed in Escherichia coli by a special DNA synthesis process termed translesion replication. This process is mutagenic due to the miscoding nature of the DNA lesions. We report that the repair enzyme formamido-pyrimidine DNA glycosylase and the general DNA damage recognition protein UvrA each inhibit specifically translesion replication through an abasic site analog by purified DNA polymerases I and II, and DNA polymerase III (alpha subunit) from E. coli. In vivo experiments suggest that a similar inhibitory mechanism prevents at least 70% of the mutations caused by ultraviolet light DNA lesions in E. coli. These results suggest that DNA damage-binding proteins regulate mutagenesis by a novel mechanism that involves direct inhibition of translesion replication. This mechanism provides anti-mutagenic defense against DNA lesions that have escaped DNA repair. |
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| Keywords |
Adenosine Triphosphatases/metabolism; Antimutagenic Agents/metabolism; Bacterial Proteins/metabolism; DNA Damage; DNA Replication; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/metabolism; DNA-Formamidopyrimidine Glycosylase; Deoxyribodipyrimidine Photo-Lyase/metabolism; Escherichia coli Proteins; Mutagenesis; N-Glycosyl Hydrolases/metabolism; Ultraviolet Rays |
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