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 p...

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Published inThe Journal of biological chemistry Vol. 268; no. 10; pp. 7401 - 7406
Main Authors Mazzei, G J, Schmid, E M, Knowles, J K, Payton, M A, Maundrell, K G
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 05.04.1993
Subjects
Amino Acid Sequence
Base Sequence
Blotting, Northern
Calcium - metabolism
DNA, Fungal
Molecular Sequence Data
Phenotype
Protein Kinase C - genetics
Protein Kinase C - metabolism
Restriction Mapping
Schizosaccharomyces - enzymology
Schizosaccharomyces - genetics
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)53188-4