In vivo and in vitro phosphorylation of DNA-binding proteins from Escherichia coli.
A deoxyribonucleoprotein (DNP) complex has been isolated from Escherichia coli cells by chromatography on Sephadex G-200. The DNP complex contains phosphoproteins and the content of phosphorus bound to the DNP protein is 3 times higher than in cytoplasmic proteins not bound to DNA. These results have been confirmed by in vivo (32-P-KH2PO4) and in vitro (32-P-ATP) phosphorylation of E. coli DNA-binding proteins isolated by chromatography on DNA--cellulose.
D001426:Bacterial Proteins / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009698:Nucleoproteins / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D009698:Nucleoproteins; D010710:Phosphates; D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases