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- W2034981642 abstract "After bacteriophage T7 infection, a protein kinase (EC 2.7.1.37; ATP:protein phosphotransferase) activity can be demonstrated in E. coli in vivo by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. Cell-free extracts catalyzed the transfer of the terminal phosphoryl group of [ γ - 32 P]ATP to endogenous protein acceptor or to added histone. The bond between phosphate and protein shows the characteristics of serine phosphate: it is stable in 1 N HCl (100°) and cleaved by 1 N KOH (37°) and by alkaline phosphatase treatment. Moreover, after partial acid hydrolysis, radiophosphate migrates with marker O -phosphoserine on polyethyleneimine-cellulose thin-layer chromatograms. Enzyme activity in uninfected cells is negligible. Ultraviolet irradiation of the phage genome prevents the appearance of the protein kinase; irradiation of the host genome does not. The enzyme activity occurs 4 min after infection and its gene maps in the early region (promoter proximal to gene 1 ). Ribosomal proteins are phosphorylated in vivo and are substrates in vitro . Enzyme activity in vitro is not changed by addition of cyclic AMP or cyclic GMP." @default.
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- W2034981642 date "1974-02-01" @default.
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- W2034981642 title "Protein Kinase Induction in <i>Escherichia coli</i> by Bacteriophage T7" @default.
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- W2034981642 doi "https://doi.org/10.1073/pnas.71.2.586" @default.
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