| Title: | Identification of a nuclear pheromone-sensitive protein kinase not identical to p34CDC28 in Saccharomyces cerevisiae |
| Author(s): | Nientiedt M; Betz R; Duntze W; |
| Address: | "Institut fur Physiologische Chemie, Ruhr Universitat, Bochum, FRG" |
| DOI: | 10.1111/j.1574-6968.1993.tb06498.x |
| ISSN/ISBN: | 0378-1097 (Print) 0378-1097 (Linking) |
| Abstract: | "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" |
| Keywords: | Cell Nucleus/*enzymology Fungal Proteins/antagonists & inhibitors/chemistry/*isolation & purification Pheromones/physiology Protein Kinase Inhibitors Protein Kinases/chemistry/*isolation & purification Saccharomyces cerevisiae/*enzymology Temperature; |
| Notes: | "MedlineNientiedt, M Betz, R Duntze, W eng Research Support, Non-U.S. Gov't England 1993/10/01 FEMS Microbiol Lett. 1993 Oct 1; 113(1):119-24. doi: 10.1111/j.1574-6968.1993.tb06498.x" |
