Format

Send to

Choose Destination
FEBS Lett. 1997 Nov 10;417(2):219-22.

Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C.

Author information

1
Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Germany.

Abstract

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.

PMID:
9395299
DOI:
10.1016/s0014-5793(97)01287-8
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center