Identification of a nuclear pheromone-sensitive protein kinase not identical to p34CDC28 in Saccharomyces cerevisiae.
Nuclei of Saccharomyces cerevisiae cells contain a protein kinase, the activity of which is drastically reduced in response to an activation of the mating signal pathway by pheromone. Inhibition of this pheromone-sensitive kinase is also observed under conditions of constitutive activation of the signal pathway in a temperature-sensitive cdc70 mutant. The enzyme, which by SDS-PAGE has a molecular mass of 34,500 Da, is a protein serine kinase that phosphorylates several endogenous substrates in nuclear extracts. The activity of this kinase is temperature-resistant in a temperature-sensitive cdc28 mutant, indicating that it is not identical to p34CDC28, the catalytic component of the cell cycle protein kinase complex.
Nientiedt
M
M
Institut für Physiologische Chemie, Ruhr Universität, Bochum, FRG.
Betz
R
R
Duntze
W
W
D002467:Cell Nucleus / Q000201:enzymology*; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D010675:Pheromones / Q000502:physiology; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000737:chemistry / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013696:Temperature
D005656:Fungal Proteins; D010675:Pheromones; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases