Application of an immunoassay to the study of yeast malate dehydrogenase inactivation

The malate dehydrogenase gene of Escherichia coli, which is susceptible to catabolite and anaerobic repression, has been cloned using plasmic pLC32-38 of Clarke and Carbon (1976). The nucleotide sequence was determined of a 2.47 kbp fragment, containing the mdh structural gene. All information necessary for expression of the mdh structural gene was mapped within a 1.3 kbp SphI-BstEII fragment. Compared with the untransformed wild type, transformations with pUC19 vector, containing this fragment, gave up to 40-fold more malate dehydrogenase activity in both E. coli wild type and mdh mutant recipients. Catabolite repression was not affected in the transformants. A possible CRP binding site in the promotor region of the mdh gene provides evidence for a co-regulation with fumA gene, the structural gene of fumarase, which is also subject to catabolite repression. The structures for transcription initiation and termination were similar to those previously described for E. coli. Amino acid sequence homologies between pro- and eucaryotic malate dehydrogenases are discussed.

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Proteolytic inactivation of the NADP-dependent glutamate dehydrogenase in proteinase-deficient mutants of Saccharomyces cerevisiae

Hemmings

Zubenko

Jones

1980

Archives of Biochemistry and Biophysics

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Application of an immunoassay to the study of yeast malate dehydrogenase inactivation

Cited by 17 publications

References 12 publications

Effect of chloroquine on proteolytic processes and energy metabolism in yeast

Effect of chloroquine on proteolytic processes and energy metabolism in yeast

Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase

Proteolytic inactivation of the NADP-dependent glutamate dehydrogenase in proteinase-deficient mutants of Saccharomyces cerevisiae

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