Mazzei G J, Schmid E M, Knowles J K, Payton M A, Maundrell K G
Glaxo Institute for Molecular Biology, Geneva, Switzerland.
J Biol Chem. 1993 Apr 5;268(10):7401-6.
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.
通过用酿酒酵母PKC1探针筛选基因组文库，从粟酒裂殖酵母中分离出一种蛋白激酶C同源物pkc1+。根据其一级序列和生化特性，我们得出结论，粟酒裂殖酵母pkc1+编码一种磷脂激活的不依赖Ca(2+)的蛋白激酶，与哺乳动物蛋白激酶C的δ/ε类同源。基因破坏实验表明，pkc1+对细胞活力不是必需的；然而，该蛋白的过表达会导致异常的细胞形态，并在有丝分裂后细胞分离受阻，提示其在细胞分裂中起作用。体外磷酸化实验揭示了几种潜在的pkc1+底物。
