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- W967144712 abstract "Ste7 functions in pheromone-induced signal transmission in Saccharomyces cerevisiae. The pheromone-induced signal causes haploid cells to arrest cell proliferation and to differentiate into a mating competent state. Five protein kinases Ste20, Ste11, Ste7, and a redundant pair of MAP kinase homologues, Fus3 and Kss1, are involved in this signal pathway. Ste7 is a dual-specificity protein kinase that activates Fus3 (and presumably Kss1) by phosphorylation on tyrosine and threonine. Ste7 is phosphorylated in response to pheromone and requires a Ste11-dependent phosphorylation for its enzyme activity. A positive regulatory domain lies within the N-terminal 45 amino acids because deletion of this region results in a stable polypeptide without catalytic activity. The sites associated with Ste7 hyperphosphorylation are located within a Ser-rich region between residues 46–17l. A derivative of Ste7 lacking the hyperphosphorylation domain is still enzymatically active. Ste7 enzyme is assayed by transfer of radioactivity from [γ32P]ATP to a catalytically inactive derivative of Fus3 (Fus3-R42). Activity of the enzyme is higher when isolated from pheromone-induced cells compared with uninduced cells. A synthetic peptide encompassing the Fus3 phosphorylation site is not phosphorylated by Ste7 under standard assay conditions." @default.
- W967144712 created "2016-06-24" @default.
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- W967144712 date "1995-01-01" @default.
- W967144712 modified "2023-09-27" @default.
- W967144712 title "Ste7" @default.
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- W967144712 doi "https://doi.org/10.1016/b978-012324719-3/50087-x" @default.
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