TY - JOUR
T1 - Binding of α-factor pheromone to yeast a cells
T2 - Chemical and genetic evidence for an α-factor receptor
AU - Jenness, Duane D.
AU - Burkholder, Anne C.
AU - Hartwell, Leland H.
N1 - Funding Information:
Thus investigation was supported by a research grant from the National Institutes of Health. D. D. J. was supported by a postdoctoral fellowship and A. C. B. by a Public Health Service tiarning grant, both from the National lnstrtutes of Health.
PY - 1983/12
Y1 - 1983/12
N2 - The division cycle of yeast a cells is inhibited by α-factor. Haploid a cells were found to bind 35S-labeled α-factor, whereas haploid α cells and diploid a/α cells showed little binding. The association of α-factor with a cells was reversible upon dilution. Unlabeled α-factor competed for binding of 35S-α-factor; the concentration dependence for competition indicated 9 × 105 binding sites per cell with a dissociation constant (KD) of 3 × 10-7 M. The rates of association (kon = 3 × 103 M-1 sec-1) and dissociation (koff = 9 × 10-4 sec-1) were consistent with the equilibrium constant. The α-factor binding activity associated with five temperature-sensitive ste2 mutants was thermolabile, suggesting that the STE2 gene encodes the receptor for α-factor. In contrast, the binding activity of other temperature-sensitive mutants (ste4, ste5, ste7, ste11, and ste12) showed no thermolability.
AB - The division cycle of yeast a cells is inhibited by α-factor. Haploid a cells were found to bind 35S-labeled α-factor, whereas haploid α cells and diploid a/α cells showed little binding. The association of α-factor with a cells was reversible upon dilution. Unlabeled α-factor competed for binding of 35S-α-factor; the concentration dependence for competition indicated 9 × 105 binding sites per cell with a dissociation constant (KD) of 3 × 10-7 M. The rates of association (kon = 3 × 103 M-1 sec-1) and dissociation (koff = 9 × 10-4 sec-1) were consistent with the equilibrium constant. The α-factor binding activity associated with five temperature-sensitive ste2 mutants was thermolabile, suggesting that the STE2 gene encodes the receptor for α-factor. In contrast, the binding activity of other temperature-sensitive mutants (ste4, ste5, ste7, ste11, and ste12) showed no thermolability.
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U2 - 10.1016/0092-8674(83)90186-1
DO - 10.1016/0092-8674(83)90186-1
M3 - Article
C2 - 6360378
AN - SCOPUS:0021070404
SN - 0092-8674
VL - 35
SP - 521
EP - 529
JO - Cell
JF - Cell
IS - 2 PART 1
ER -