Phosphate-containing proteins of Salmonella typhimurium and Escherichia coli. Analysis by a new two-dimensional gel system.
The pattern of post-translational protein modifications involving a phosphate group was determined in the prokaryotes Salmonella typhimurium and Escherichia coli. A special two-dimensional gel electrophoretic separation was developed which utilizes acidic urea in the first dimension and neutral sodium dodecyl sulfate in the second dimension. This system allows survival and visualization of a number of proteins which are otherwise lost in systems employing basic conditions. The total number of phosphate-containing proteins thus obtained is approximately twenty. Among them are included proteins containing nucleotidylyl groups; two of these have been identified: glutamine synthetase (adenylylated) and regulatory protein PII (uridylylated). Two phosphate-containing proteins are shown to be regulated by the level of K+. The pattern of phosphorylation is shown to change with changing growth conditions and with specific mutations.
D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004926:Escherichia coli / Q000378:metabolism*; D010750:Phosphoproteins / Q000032:analysis / Q000378:metabolism*; D010766:Phosphorylation; D012486:Salmonella typhimurium / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate
D010750:Phosphoproteins; D012967:Sodium Dodecyl Sulfate