In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of Escherichia coli by bacteriophage-T7-induced protein kinase.
After infection with bacteriophage T7 the beta' and to a lesser extent the beta subunits of E. coli DNA-dependent RNA polymerase (nucleosidetriphosphate:RNA nucleotidyltransferase, EC 2.7.7.6) are phosphorylated by a phage-gene-encoded protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37). The phosphorylation occurs on threonine residues and appears site-specific. It is probably the molecular basis of the early transcriptional control.
D003090:Coliphages / Q000201:enzymology*; D004247:DNA; D004267:DNA Viruses / Q000201:enzymology; D012321:DNA-Directed RNA Polymerases / Q000276:immunology / Q000378:metabolism*; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D010750:Phosphoproteins / Q000096:biosynthesis; D011233:Precipitin Tests; D011494:Protein Kinases / Q000378:metabolism*
D010750:Phosphoproteins; D004247:DNA; D011494:Protein Kinases; D012321:DNA-Directed RNA Polymerases