Characterization of eukaryotic-like kinase activity in Escherichia coli using the gene-protein database.
The gene-protein database was used to obtain the two-dimensional polyacrylamide gel coordinates of proteins phosphorylated in extracts of Escherichia coli including those phosphorylated by eukaryotic-like kinase activities. These suggest that the phosphoproteins correspond to, or co-migrate with, the product of an open reading frame at 1.3 min (Orf80), Enzyme 1 of the phosphoenolpyruvate-dependent phosphotransferase system (PtsI), the tRNA synthetase for histidine (HisS), and proteins involved in the response to carbon starvation and quinone treatment.
Sweeney
S T
ST
Department of Microbiology and Immunology, University of Leicester, UK.
Freestone
P
P
Norris
V
V
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016208:Databases, Factual; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D005057:Eukaryotic Cells; D016366:Open Reading Frames; D010750:Phosphoproteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D010750:Phosphoproteins; D011494:Protein Kinases