A Ca(2+)-independent protein kinase C from fission yeast.
A protein kinase C homologue of Schizosaccharomyces pombe, pkc1+, was isolated from a genomic library by screening with the Saccharomyces cerevisiae PKC1 probe. From its primary sequence and biochemical properties, we conclude that S. pombe pkc1+ encodes a phospholipid-activated Ca(2+)-independent protein kinase, homologous to the delta/epsilon classes of mammalian protein kinase C. Gene disruption experiments show that pkc1+ is not essential for cell viability; however, overexpression of the protein leads to an abnormal cell morphology and a block in cell separation following mitosis suggestive of a role in cell division. In vitro phosphorylation experiments reveal several potential pkc1+ substrates.
Mazzei
G J
GJ
Glaxo Institute for Molecular Biology, Geneva, Switzerland.
Schmid
E M
EM
Knowles
J K
JK
Payton
M A
MA
Maundrell
K G
KG
D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D002118:Calcium / Q000378:metabolism*; D004271:DNA, Fungal; D008969:Molecular Sequence Data; D010641:Phenotype; D011493:Protein Kinase C / Q000235:genetics / Q000378:metabolism*; D015183:Restriction Mapping; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000235:genetics
D004271:DNA, Fungal; D011493:Protein Kinase C; D002118:Calcium