Behme M T, Lilley G D, Ebisuzaki K
J Virol. 1976 Apr;18(1):20-5. doi: 10.1128/JVI.18.1.20-25.1976.
Infection by bacteriophage T4 has previously been shown to cause a rapid inhibition of the host recBC DNase, an ATP-dependent DNase that is required for genetic recombination in Escherichia coli. We report here the partial purification of a protein ("T4 rec inhibitor") from extracts of T4-infected cells and some characteristics of the in vitro inhibition reaction with purified inhibitor and recBC nuclease. This inhibitory activity could not be purified from extracts of uninfected E. coli. Both the ATP-dependent exonuclease and DNA-dependent ATPase activities of recBC DNase are inhibited by T4 rec inhibitor. Experiments suggest that the inhibitor interacts with the nuclease in a stoichiometric manner. The biological significance of this inhibition is discussed with respect to control reactions in phage-infected cells.
先前已表明,噬菌体T4感染会导致宿主recBC DNA酶迅速受到抑制,recBC DNA酶是一种ATP依赖性DNA酶,大肠杆菌的基因重组需要它。我们在此报告了从T4感染细胞提取物中部分纯化出一种蛋白质(“T4 rec抑制剂”),以及用纯化的抑制剂和recBC核酸酶进行体外抑制反应的一些特性。未感染的大肠杆菌提取物中无法纯化出这种抑制活性。recBC DNA酶的ATP依赖性核酸外切酶活性和DNA依赖性ATP酶活性均受到T4 rec抑制剂的抑制。实验表明,抑制剂与核酸酶以化学计量方式相互作用。针对噬菌体感染细胞中的控制反应,讨论了这种抑制作用的生物学意义。