title: 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.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D011232:Chemical Precipitation; D002701:Chloramphenicol / Q000494:pharmacology; D002845:Chromatography; D003090:Coliphages / Q000032:analysis* / Q000254:growth & development; D004267:DNA Viruses; D004926:Escherichia coli / Q000201:enzymology*; D005092:Exonucleases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008970:Molecular Weight; D014764:Viral Proteins / Q000302:isolation & purification / Q000494:pharmacology
chemical_list: D014764:Viral Proteins; D002701:Chloramphenicol; D005092:Exonucleases; D000251:Adenosine Triphosphatases