A protein kinase C-like activity in Escherichia coli.
The protein kinase C (PKC) family comprises calcium- and phospholipid-dependent kinases whose activity is stimulated by diacylglycerol and tumour-promoting phorbol esters such as 12-tetradecanoyl phorbol-13-acetate (TPA). In the Gram-negative bacterium Escherichia coli, functional similarity to PKC was demonstrated in crude extracts by calcium and phospholipid-dependent, TPA-stimulated phosphorylation of a small number of endogenous substrates. Activity was reduced by sphingosine, a known inhibitor of eukaryotic PKC. Structural similarity to PKC was demonstrated in crude and partially purified bacterial extracts by cross-reactivity with several monoclonal antibodies. This revealed isozyme-specific homology between a protein(s) of relative molecular mass 80-85,000 in E. coli and the alpha- and gamma-isozymes, but probably not the beta-isozyme, of eukaryotic PKC.
Norris
V
V
Department of Genetics, University of Leicester, UK.
Baldwin
T J
TJ
Sweeney
S T
ST
Williams
P H
PH
Leach
K L
KL
D000911:Antibodies, Monoclonal; D002118:Calcium / Q000494:pharmacology; D003429:Cross Reactions; D004075:Diglycerides / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D007527:Isoenzymes; D011493:Protein Kinase C / Q000187:drug effects / Q000276:immunology / Q000378:metabolism*; D013110:Sphingosine / Q000494:pharmacology; D013379:Substrate Specificity; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D004075:Diglycerides; D007527:Isoenzymes; D011493:Protein Kinase C; D013110:Sphingosine; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium