Abstract
Mutations in the uvrD gene of Escherichia coli K-12 result in multiple phenotypes, including increased sensitivity to UV light and ionizing radiation, decreased ability for host cell reactivation, increased spontaneous mutation frequency and decreased rate of genetic recombination1–6. It has been shown, moreover, that double mutants having mutations in both uvrD and polA genes are conditionally lethal7–10. The pleiotropic phenotypes of the uvrD mutants suggest that the uvrD gene product may have important roles in the processes of DNA repair, recombination and replication. To study the function of the uvrD gene, we have constructed hybrid phages and plasmids that carry the gene11. Here we have analysed the proteins synthesized by the hybrid phages and report that the uvrD gene product is a polypeptide of molecular weight (MW) 75,000. We present evidence that the uvrD protein possesses a DNA-dependent ATPase activity.
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