Tyrosine phosphorylation of a yeast 40 kDa protein occurs in response to mating pheromone.
AUTOR(ES)
Ballard, M J
RESUMO
Tyrosine phosphorylation of proteins in the yeast Saccharomyces cerevisiae has been examined following exposure to the mating pheromone alpha-factor. When a cells are treated with alpha-factor a protein of approximately 40 kDa molecular weight is tyrosine phosphorylated. This tyrosine phosphorylation response requires an intact signal transduction pathway, is not restricted to a short interval of the cell division cycle, and requires protein synthesis for its maximal accumulation. Mating competent fus3 deletion strains fail to elaborate the phosphotyrosine response. The possibility that FUS3 encodes the 40 kDa protein is discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=453111Documentos Relacionados
- Determinants for binding of a 40 kDa protein to the leaders of yeast mitochondrial mRNAs.
- Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.
- FAR1 is required for posttranscriptional regulation of CLN2 gene expression in response to mating pheromone.
- Yeast pheromone response pathway: characterization of a suppressor that restores mating to receptorless mutants.
- Localized deposition of chitin on the yeast cell surface in response to mating pheromone