1. Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors
- Author
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Johan A. Van Den Berg, G. Paul H. van Heusden, H. Y. De Steensma, Ellen Lagendijk, and Thibaut José Wenzel
- Subjects
Saccharomyces cerevisiae Proteins ,Tyrosine 3-Monooxygenase ,LRP1B ,Genes, Fungal ,Molecular Sequence Data ,Restriction Mapping ,Biophysics ,Nerve Tissue Proteins ,Saccharomyces cerevisiae ,Biology ,Acetates ,SYT1 ,Biochemistry ,Fungal Proteins ,Transformation, Genetic ,Structural Biology ,Protein kinase C ,Sequence Homology, Nucleic Acid ,HSPA2 ,SNAP23 ,Genetics ,Escherichia coli ,Animals ,Amino Acid Sequence ,Cloning, Molecular ,DNA, Fungal ,Molecular Biology ,Protein kinase II ,Acetic Acid ,Sheep ,Base Sequence ,14-3-3 protein ,Cell Biology ,Autophagy-related protein 13 ,Blotting, Northern ,Molecular biology ,GPS2 ,Enzyme Activation ,Glucose ,14-3-3 Proteins ,Mutagenesis ,AKT1S1 ,RNA ,Cattle ,Cyclin-dependent kinase 7 ,Protein Kinases ,Plasmids - Abstract
We describe the identification and characterization of the BMH1 gene from the yeast Saccharomyces cerevisiae. The gene encodes a putative protein of 292 amino acids which is more than 50% identical with the bovine brain 14-3-3 protein and proteins isolated from sheep brain which are strong inhibitors of protein kinase C. Disruption mutants and strains with the BMH1 gene on multicopy plasmids have impaired growth on minimal medium with glucose as carbon source, i.e. a 30–50% increase in generation time. These observations suggest a regulatory function of the bmh1 protein. In contrast to strains with an intact or a disrupted BMH1 gene, strains with the BMH1 gene on multicopy plasmids hardly grew on media with acetate or glycerol as carbon source.
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