Protein kinase of bacteriophage T7 induces the phosphorylation of only a small number of proteins in the infected cell》.pdf

VIROLOGY 175,%?5-534 (1990) Protein Kinase of Bacteriophage T7 Induces the Phosphorylation of Only a Small Number of Proteins in the Infected Cell ERLE S. ROBERTSON AND ALLEN W. NICHOLSON’ Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202 Received August 23, 1989; accepted December 27, 1989 Bacteriophage T7 expresses a serine/threonine-specific, CAMP-independent protein kinase activity encoded by the early gene 0.7. The phosphoproteins specifically resulting from gp0.7 protein kinase expression in T7-infected Ese- richia co/i have been examined by one-dimensional, SDS-polyacrylamide gel electrophoresis. Only seven major, stable phosphoproteins dependent on gp0.7 protein kinase expression are observed. Two of the gp0.7 protein kinase-specific phosphoproteins observed have been previously identified: the fl subunit of RNA polymerase and the RNA processing enzyme RNase Ill. The gp0.7-catalyzed protein phosphorylation activity appears at 9-l 1 min postinfection at 30’. The new phosphoproteins have a metabolic stability comparable to that of uninfected cell phosphoproteins. T7 protein kinase expression causes the phosphorylation of the same, limited set of proteins in B, C, or K strains of E. co/i. Expres- sion of the T3 and BA14 phage protein kinase activities also produces the same phosphoproteins. cc