Abstract
Data have been presented indicating that gene 56 of bacteriophage T4 controls the synthesis of both the phage-induced dCTPase and dUTPase activities. Fractionation of extracts of phage-infected cells with streptomycin sulfate, DEAE-cellulose chromatography, and hydroxylapatite chromatography indicated that these two activities probably reside in the same protein. Mutual inhibition studies indicated that the same site may catalyze both reactions. Furthermore, the purified enzyme also hydrolyzes dUDP, and this dUDPase activity is not induced in E. coli by gene 56 mutants. The dUDP inhibits dCTP hydrolysis, suggesting that there is a common catalytic site for dUTP, dCTP, and dUDP hydrolysis on the phage-induced enzyme. The results of others would imply that dCDP is also hydrolyzed at this site.