Abstract
The synthesis of β-galactosidase (EC 3.2.1.23: β-D-galactoside galactohydrolase) in Escherichia coli is repressed as a result of infection with single-stranded DNA phage ØX174. An amber mutant in ØX174 cistron A, which codes for two proteins, does not inhibit the enzyme synthesis while amber mutants in all other genes do cause repression. A mutant near the amino-terminal end of cistron A, which produces the small 35,000 molecular weight cistron A polypeptide, also inhibits the synthesis of β-galactosidase. Inhibition is also observed in an Escherichia coli rep mutant which does not support the replication of replicative-form DNA. Exogenous nucleotide bases and cyclic 3′,5′-adenosine monophosphate (cyclic AMP) do not have any effect on the degree of repression.
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