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Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C
Author(s) -
Jacoby Jörg J,
Schmitz Hans-Peter,
Heinisch Jürgen J
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01287-8
Subject(s) - saccharomyces cerevisiae , yeast , biochemistry , diacylglycerol kinase , mutant , cysteine , protein kinase c , biology , site directed mutagenesis , mutagenesis , staurosporine , enzyme , gene
In an attempt to study the functional similarities between protein kinase C from the yeast Saccharomyces cerevisiae and its human homologues we have started in vitro mutagenesis to alter specific domains. Here we report on the exchange of four cysteine residues by serines in yeast Pkc1p that have been shown to be essential for diacylglycerol (DAG) binding and activation by this compound in humans. The mutant yeast protein leads to sensitivity to caffeine and low concentrations of SDS when expressed in a pkc1 deletion strain. However, sensitivity to staurosporine was not affected. Our data indicate that the conserved DAG binding domain serves an important function in yeast Pkc1p.