The purpose of the given work was the experimental analysis of features of Arg-X proteolysis in proteom of supramolecular structures of bacterial cells during their life cycle. The basic attention was devoted to relax...The purpose of the given work was the experimental analysis of features of Arg-X proteolysis in proteom of supramolecular structures of bacterial cells during their life cycle. The basic attention was devoted to relaxation of Arg-X sites of proteom in association with the evolutionary significance ofArg-rich histones in the eukaryotic kingdom. These properties were not studied in the prokaryotes. Cells ofE. coli were grown to the stationary phase, collected by centrifugation and washed. All cells were taken over from 50 min to 430 min at intervals of 20 min and were preserved in glycerol. The supramolecular structures were fractionated from bacterial cells by increasing ionic strength of solution. The Arg-Xactivity was assessed by cleavage of Arg-Xbonds in the arginine-enriched protein protamine in all cell fractions. We have shown that during the stationary phase in the life cycle of E. coli, there are a high continuous activity of the Arg-X processing at the level of＂cytoskeleton＂ of the cell and bright cyclic activity in the cytoplasm.展开更多
文摘The purpose of the given work was the experimental analysis of features of Arg-X proteolysis in proteom of supramolecular structures of bacterial cells during their life cycle. The basic attention was devoted to relaxation of Arg-X sites of proteom in association with the evolutionary significance ofArg-rich histones in the eukaryotic kingdom. These properties were not studied in the prokaryotes. Cells ofE. coli were grown to the stationary phase, collected by centrifugation and washed. All cells were taken over from 50 min to 430 min at intervals of 20 min and were preserved in glycerol. The supramolecular structures were fractionated from bacterial cells by increasing ionic strength of solution. The Arg-Xactivity was assessed by cleavage of Arg-Xbonds in the arginine-enriched protein protamine in all cell fractions. We have shown that during the stationary phase in the life cycle of E. coli, there are a high continuous activity of the Arg-X processing at the level of＂cytoskeleton＂ of the cell and bright cyclic activity in the cytoplasm.
