• Media type: E-Article
  • Title: Two alanine aminotranferases link mitochondrial glycolate oxidation to the major photorespiratory pathway inArabidopsisand rice
  • Contributor: Niessen, Markus; Krause, Katrin; Horst, Ina; Staebler, Norma; Klaus, Stephanie; Gaertner, Stefanie; Kebeish, Rashad; Araujo, Wagner L.; Fernie, Alisdair R.; Peterhansel, Christoph
  • Published: Oxford University Press, 2012
  • Published in: Journal of Experimental Botany, 63 (2012) 7, Seite 2705-2716
  • Language: English
  • ISSN: 0022-0957; 1460-2431
  • Keywords: RESEARCH PAPER
  • Origination:
  • Footnote:
  • Description: Abstract The major photorespiratory pathway in higher plants is distributed over chloroplasts, mitochondria, and peroxisomes. In this pathway, glycolate oxidation takes place in peroxisomes. It was previously suggested that a mitochondrial glycolate dehydrogenase (GlcDH) that was conserved from green algae lacking leaf-type peroxisomes contributes to photorespiration inArabidopsis thaliana. Here, the identification of twoArabidopsismitochondrial alanine:glyoxylate aminotransferases (ALAATs) that link glycolate oxidation to glycine formation are described. By this reaction, the mitochondrial side pathway produces glycine from glyoxylate that can be used in the glycine decarboxylase (GCD) reaction of the major pathway. RNA interference (RNAi) suppression of mitochondrial ALAAT did not result in major changes in metabolite pools under standard conditions or enhanced photorespiratroy flux, respectively. However, RNAi lines showed reduced photorespiratory CO₂ release and a lower CO₂ compensation point. Mitochondria isolated from RNAi lines are incapable of converting glycolate to CO₂, whereas simultaneous overexpression of GlcDH and ALAATs in transiently transformed tobacco leaves enhances glycolate conversion. Furthermore, analyses of rice mitochondria suggest that the side pathway for glycolate oxidation and glycine formation is conserved in monocotyledoneous plants. It is concluded that the photorespiratory pathway from green algae has been functionally conserved in higher plants.
  • Access State: Open Access