Abstract
A protein (molecular mass 66 kDa) that bound cAMP in a highly specific manner was purified to electrophoretic homogeneity from yeast cells of the important opportunistic fungal pathogen Candida albicans . The protein was identified as a regulatory subunit of a cAMP-dependent protein kinase (protein kinase A; PKA) when it was incubated with protein kinase activity partly purified from C. albicans : phosphotransferase activity was inhibited in a dose-dependent manner and the inhibition was readily reversed by the addition of cAMP. In general, the substrate specificity of the C. albicans PKA catalytic subunit reflected that observed for other PKAs. Furthermore, enzyme activity was sensitive to the specific and potent inhibitor of mammalian PKAs, PKI 6–22′ and the C. albicans regulatory subunit inhibited bovine PKA catalytic subunit activity. These results indicate a high level of evolutionary conservation of the genes encoding PKA regulatory and catalytic subunits.
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