ENZYME COMPLEMENTATION IN VITRO BETWEEN ADENYLOSUCCINASELESS MUTANTS OF NEUROSPORA CRASSA

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Abstract
In vitro complementation between homogenates from Neurospora adenylosuccinaseless mutants resulting in restored adenylosuccinase activity is described. As much as 20% of the activity recovered from in vivo complementation in heterocaryons has been restored by the in vitro mixing procedure. If the homogenates from 2 complementing mutants are not mixed immediately after the mycelia have been disrupted, enzyme activity is not recovered. No enzyme activity has been detected when homogenates from non-complementing mutants are mixed. In vivo complementation results in the restoration of enzyme activity to a maximum level not exceeding 25% of wild type. There is a direct correlation between enzyme activity recovered from interallelic heterocaryons and distance between the mutant components on the complementation map. These results support the hypothesis previously proposed that, in general, interallelic complementation in enzyme formation involves a cytoplasmic exchange mechanism resulting in the formation of hybrid protein.

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