Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8291993 | Archives of Biochemistry and Biophysics | 2008 | 8 Pages |
Abstract
Yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase (idhÎ) or aconitase (aco1Î) were found to share several growth phenotypes as well as patterns of specific protein expression that differed from the parental strain. These shared properties of idhÎ and aco1Î strains were eliminated or moderated by co-disruption of the CIT1 gene encoding mitochondrial citrate synthase. Gas chromatography/mass spectrometry analyses indicated a particularly dramatic increase in cellular citrate levels in idhÎ and aco1Î strains, whereas citrate levels were substantially lower in idhÎcit1Î and aco1Îcit1Î strains. Exogenous addition of citrate to parental strain cultures partially recapitulated effects of high endogenous levels of citrate in idhÎ and aco1Î strains. Finally, effects of elevated cellular citrate in idhÎ and aco1Î mutant strains were partially alleviated by addition of iron or by an increase in pH of the growth medium, suggesting that detrimental effects of citrate are due to elevated levels of the ionized form of this metabolite.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
An-Ping Lin, Kevin W. Hakala, Susan T. Weintraub, Lee McAlister-Henn,