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. 1991 Dec;10(12):3753–3758. doi: 10.1002/j.1460-2075.1991.tb04944.x

Tyrosine phosphorylation of a yeast 40 kDa protein occurs in response to mating pheromone.

M J Ballard 1, W A Tyndall 1, J M Shingle 1, D J Hall 1, E Winter 1
PMCID: PMC453111  PMID: 1935898

Abstract

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.

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