Peroxisomal localization and function of NADP+-specific isocitrate dehydrogenases in yeast

Qian Lu, Lee McAlister-Henn

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Yeast peroxisomal NADP+-specific isocitrate dehydrogenase (IDP3) contains a canonical type I peroxisomal targeting sequence (a carboxyl-terminal Cys-Lys-Leu tripeptide), and provides the NADPH required for β-oxidation of some fatty acids in that organelle. Cytosolic yeast IDP2 carrying a PTS1 (IDP2+CKL) was only partially localized to peroxisomes, and the enzyme was able to function in lieu of either peroxisomal IDP3 or cytosolic IDP2. The analogous isocitrate dehydrogenase enzyme (IDPA) from Aspergillus nidulans, irrespective of the presence or absence of a putative PTS1, was found to exhibit patterns of dual compartmental distribution and of dual function in yeast similar to those observed for IDP2+CKL. To test a potential cellular limit on peroxisomal levels, authentic yeast IDP3, which is normally strictly peroxisomal, was over-expressed. This also resulted in dual distribution and function of the enzyme in both the cytosol and in peroxisomes, supporting the possibility of a restriction on organellar amounts of IDP.

Original languageEnglish (US)
Pages (from-to)125-134
Number of pages10
JournalArchives of Biochemistry and Biophysics
Volume493
Issue number2
DOIs
Publication statusPublished - Jan 15 2010

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Keywords

  • Antioxidant
  • Isocitrate dehydrogenase
  • NADP(H)
  • Peroxisomes
  • β-Oxidation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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