Summary: The gene of serovar strain kenniwicki has been cloned on a 9.5 kb plasmid, pWVL1, by complementation of mutants. Subcloning and Tn5 mutagenesis showed that the region required for complementation was approximately 1.2 kb in length. Enzyme assays showed that the product of the cloned gene was a β-isopropylmalate dehydrogenase. Defects in the and genes of were not complemented by pWVL1. The nucleotide sequence of the -complementing region and surrounding DNA has been determined. Three open reading frames were found which encode proteins of 40.9, 38.8 and 15 kDa. Analysis of subclones containing nucleotide deletions of varying sizes showed that only the 38.8 kDa protein was necessary to obtain complementation of mutations. The PIR data base was searched and the enzyme 3-isopropylmalate dehydrogenase from six different micro-organisms was found to share significant amino acid sequence similarity (43-57%) with the 38.8 kDa gene product. The organization of the leucine biosynthetic genes in differs from that found in and


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