The immunological properties of ten lipoamide dehydrogenase mutants of were investigated with antiserum raised against purified lipoamide dehydrogenase. Seven mutants were CRM+ (cross-reacting material present) as they contained lipoamide dehydrogenase proteins exhibiting either complete or partial immunological identity with the wild-type protein. This indicates that at least seven of the mutations affect the lipoamide dehydrogenase structural gene (). The remaining three mutants (CRM-) contained no detectable cross-reacting protein. None of the mutations were sensitive to any of three different -suppressors. Genetic analysis by P1-transduction showed that all the mutant sites were clustered very near the distal gene () of the region which specifies the dehydrogenase () and transacetylase () components of the pyruvate dehydrogenase multienzyme complex. Calculations based on the recombination frequency between an mutant and the nearest mutant site support the conclusion that apart from the possible presence of a regulatory element, the and genes are contiguous.


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