Protein kinase induction in Escherichia coli by bacteriophage T7.
作者： H. J. Rahmsdorf , S. H. Pai , P. Ponta , P. Herrlich , R. Roskoski
关键词: Biochemistry 、 Phosphotransferase 、 Gel electrophoresis 、 Escherichia coli 、 Kinase 、 Protein kinase A 、 Molecular biology 、 Adenosine triphosphate 、 Alkaline phosphatase 、 Biology 、 Enzyme inducer
摘要: After bacteriophage T7 infection, a protein kinase (EC 2.7.1.37; ATP:protein phosphotransferase) activity can be demonstrated in E. coli vivo by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. Cell-free extracts catalyzed the transfer of terminal phosphoryl group [(gamma)-(32)P]ATP to endogenous acceptor or added histone. The bond between phosphate shows characteristics serine phosphate: it is stable 1 N HCl (100 degrees ) cleaved KOH (37 alkaline phosphatase treatment. Moreover, after partial acid hydrolysis, radiophosphate migrates with marker O-phosphoserine on polyethyleneimine-cellulose thin-layer chromatograms. Enzyme uninfected cells negligible. Ultraviolet irradiation phage genome prevents appearance kinase; host does not. enzyme occurs 4 min infection its gene maps early region (promoter proximal 1). Ribosomal proteins are phosphorylated substrates vitro. vitro not changed addition cyclic AMP GMP.
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