NUCLEASE ACTIVITY IN DEFECTIVE LYSOGENS OF PHAGE λ, II. A HYPERACTIVE MUTANT

Publisher Website
Google Scholar
Abstract
Among the early defective lysogens of Jacob, one, T11 ([lambda] t11), has been found which is five times more active than wild type with respect to the rate of appearance and at least ten times more active with respect to the total yield of nuclease activity which appears after induction. The capacity for increased enzymatic activity was transferred to the other strains of E. coli K12 with the defective prophage. In the double lysogens C600([lambda]cI, [lambda]T11) and W3350-( [lambda] cI, [lambda]T11) the phenotypic expression of [lambda]t11 was found to be inhibted 85 per cent. Studies on the partial purification of nuclease from T11( [lambda] T11) indicate that the increased activity is assignable to an enzyme or enzymes whose properties are similar to those reported for nuclease purified from a wild-type lysogen.