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The activity of uracil-DNA glycosylase in Escherichia coli decreases dramatically to less than 10% of its original level after infection of the cells by phage T5. Phage-induced protein synthesis is required for this inhibition to occur, and the inhibition is induced by a mutant capable of injecting only the first 8% of its DNA. The inhibitor activity in extracts of infected cells is heat labile and nondialyzable, and will inhibit enzyme activity present in extracts of uninfected cells.
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Warner et al. (1980) studied this question.
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