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The identification and purification of a mammalian-like protein kinase C in the yeast Saccharomyces cerevisiae



The identification and purification of a mammalian-like protein kinase C in the yeast Saccharomyces cerevisiae



Proceedings. Biological Sciences 243(1307): 165-171



We have purified a yeast protein kinase that is phospholipid-dependent and activated by Diacylglycerol (DAG) in the presence of Ca2+ or by the tumour-promoting agent tetradecanoyl-phorbol acetate (TPA). The properties of this enzyme are similar to those of the mammalian protein kinase C (PKC). The enzyme was purified using chromatography on DEAE-cellulose followed by hydroxylapatite. The latter chromatography separated the activity to three distinguishable sub-species, analogous to the mammalian PKC isoenzymes. The fractions enriched in PKC activity contain proteins that specifically bind TPA, are specifically phosphorylated in the presence of DAG and recognized by anti-mammalian PKC antibodies.

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Accession: 041665917

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PMID: 1676520

DOI: 10.1098/rspb.1991.0027


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