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J. Biol. Chem., Vol. 266, Issue 33, 22199-22205, Nov, 1991
JR Cupp and L McAlister-Henn
NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae is
composed of two nonidentical subunits, designated IDH1 (Mr approximately
40,000) and IDH2 (Mr approximately 39,000). We have isolated and
characterized a yeast genomic clone containing the IDH2 gene. The amino
acid sequence deduced from the gene indicates that IDH2 is synthesized as a
precursor of 369 amino acids (Mr 39,694) and is processed upon
mitochondrial import to yield a mature protein of 354 amino acids (Mr
37,755). Amino acid sequence comparison between S. cerevisiae IDH2 and S.
cerevisiae NADP(+)-dependent isocitrate dehydrogenase shows no significant
sequence identity, whereas comparison of IDH2 and Escherichia coli
NADP(+)-dependent isocitrate dehydrogenase reveals a 33% sequence identity.
To confirm the identity of the IDH2 gene and examine the relationship
between IDH1 and IDH2, the IDH2 gene was disrupted by genomic replacement
in a haploid yeast strain. The disruption strain expressed no detectable
IDH2, as determined by Western blot analysis, and was found to lack NAD(+)-
dependent isocitrate dehydrogenase activity, indicating that IDH2 is
essential for a functional enzyme. Overexpression of IDH2, however, did not
result in increased NAD(+)-dependent isocitrate dehydrogenase activity,
suggesting that both IDH1 and IDH2 subunits are required for catalytic
activity. The disruption strain was unable to utilize acetate as a carbon
source and exhibited a 2-fold slower growth rate than wild type strains on
glycerol or lactate. This growth phenotype is consistent with
NAD(+)-dependent isocitrate dehydrogenase performing an essential role in
the oxidative function of the citric acid cycle.
NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae
Department of Biological Chemistry, University of California, Irvine 92717.
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