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

Qian Lu, Lee McAlister-Henn

Resultado de la investigación: Articlerevisión exhaustiva

13 Citas (Scopus)


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.

Idioma originalEnglish (US)
Páginas (desde-hasta)125-134
Número de páginas10
PublicaciónArchives of Biochemistry and Biophysics
EstadoPublished - ene 15 2010

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


Profundice en los temas de investigación de 'Peroxisomal localization and function of NADP+-specific isocitrate dehydrogenases in yeast'. En conjunto forman una huella única.

Citar esto