Partial purification and properties of a bacteriophage T7 inhibitor of the host exonuclease V activity

Abstract

Infection of Escherichia coli with bacteriophage T7 results in an inhibition of the host exonuclease V (recB, C DNase) activity. This inhibition is not observed when cells are infected in the presence of chloramphenicol or with a gene 1 mutant. The protein responsible for the inhibition of exonuclease V has been partially purified from T7-infected cells. The protein which does not possess nuclease or ATPase activity can inhibit all nucleolytic activities associated with exonuclease V. The protein does not, however, inhibit the DNA-dependent ATPase activity associated with exonuclease V. The inhibitory protein has a molecular weight of about 12,000, as determined from sedimentation analysis in glycerol gradients.