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J. Biol. Chem., Vol. 269, Issue 31, 19817-19825, Aug, 1994
GA Caldwell, SH Wang, CB Xue, Y Jiang, HF Lu, F Naider and JM Becker
The a-factor of Saccharomyces cerevisiae (YIIKGVF-WDPAC(Farnesyl)-OCH3) is
a peptide pheromone in which post-translational modification with a
farnesyl isoprenoid and carboxyl methyl group is required for export and
bioactivity. Truncated and carboxyl-terminal modified analogs of the
a-factor were synthesized in order to determine the effect of such
modifications on bioactivity. Bioactivity studies on carboxyl-terminal
analogs in which the chirality, the cysteine thioether, and the carboxyl
ester were varied in an attempt to study the influence of topology on
a-factor activity indicate that the hydrophobicity conferred by the
farnesyl moiety and not its specific spatial orientation is a key
determinant of a-factor potency. Analyses on truncated a-factors suggest
that sequential removal of NH2-terminal residues leads to a gradient of
potency loss, with some amino acids exhibiting a slightly greater
contribution to bioactivity than others. Random oligonucleotide-targeted
mutagenesis of the gene encoding a- factor was coupled to a biological
screen to identify altered a-factor peptides which are secreted yet exhibit
a loss of a-factor bioactivity. Transformants exhibiting this phenotype
were examined to identify codon changes presumably responsible for the
altered phenotype, thus indicating residues that may contribute
significantly to a-factor bioactivity.
Molecular determinants of bioactivity of the Saccharomyces cerevisiae lipopeptide mating pheromone
Program in Cellular, Molecular, and Developmental Biology, University of Knoxville 37996-0845.
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