Open AccessIdentification of a nuclear pheromone‐sensitive protein kinase not identical to p34 CDC28 in Saccharomyces cerevisiae
Author(s) -
Nientiedt Marietta,
Betz Richard,
Duntze Wolfgang
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06498.x
Subject(s) - saccharomyces cerevisiae , biochemistry , chemistry , identification (biology) , pheromone , protein kinase a , biology , kinase , genetics , yeast , botany
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 34500 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 p34 CDC28 , the catalytic component of the cell cycle protein kinase complex.