Abstract
Two different types of allelic complementation were observed in tryptophan synthetase mutants of the yeast Saccharomyces cerevisiae. Each type is associated with a different mechanism for the enzymatic conversion of indole-3-glycerol phosphate (InGP) to tryptophan. Mechanism I is utilized by a hybrid tryptophan synthetase that resembles, but is not identical with, the wild-type enzyme. Mechanism II is due to a sequential conversion of InGP to free indole, and indole to tryptophan. Two partially active mutant enzymes rather than a single hybrid enzyme catalyze the sequential reaction steps. This is an example of intracellular cross-feeding. The quantitative evaluation of mechanism II leads to the conclusion that tryptophan synthetase in yeast is most likely a dimer of two identical subunits.
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