Dual compartmental localization and function of mammalian NADP+-specific isocitrate dehydrogenase in yeast

Qian Lu, Karyl I. Minard, Lee McAlister-Henn

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Isozymes of NADP+-specific isocitrate dehydrogenase (IDP) provide NADPH in cytosolic, mitochondrial, and peroxisomal compartments of eukaryotic cells. Analyses of purified IDP isozymes from yeast and from mouse suggest a general correspondence of pH optima for catalysis and pI values with pH values reported for resident cellular compartments. However, mouse IDP2, which partitions between cytosolic and peroxisomal compartments in mammalian cells, exhibits a broad pH optimum and an intermediate pI value. Mouse IDP2 was found to similarly colocalize in both cellular compartments when expressed in yeast at levels equivalent to those of endogenous yeast isozymes. The mouse enzyme can compensate for loss of yeast cytosolic IDP2 and of peroxisomal IDP3. Removal of the peroxisomal targeting signal of the mouse enzyme precludes both localization in peroxisomes and compensation for loss of yeast IDP3.

Original languageEnglish (US)
Pages (from-to)17-25
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume472
Issue number1
DOIs
StatePublished - Apr 1 2008

Keywords

  • Compartmentalization
  • Isocitrate dehydrogenase
  • NADPH
  • Saccharomyces cerevisiae
  • β-Oxidation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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