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A protein kinase C‐like activity in Escherichia coli
Author(s) -
Norris V.,
Baldwin T. J.,
Sweeney S. T.,
Williams P. H.,
Leach K. L.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb01857.x
Subject(s) - protein kinase c , biology , diacylglycerol kinase , isozyme , escherichia coli , biochemistry , sphingosine , phorbol , kinase , phospholipid , enzyme , phosphorylation , microbiology and biotechnology , receptor , gene , membrane
Summary 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 80–85000 in E. coli and the α‐and γ‐isozymes, but probably not the β‐isozyme, of eukaryotic PKC.