Author
Listed:
- Youjun Zhang
(Max-Planck-Institut für Molekulare Pflanzenphysiologie
Center of Plant Systems Biology and Biotechnology)
- Arun Sampathkumar
(Max-Planck-Institut für Molekulare Pflanzenphysiologie)
- Sandra Mae-Lin Kerber
(Max-Planck-Institut für Molekulare Pflanzenphysiologie)
- Corné Swart
(Max-Planck-Institut für Molekulare Pflanzenphysiologie)
- Carsten Hille
(University of Potsdam
Technical University of Applied Sciences Wildau)
- Kumar Seerangan
(Max-Planck-Institut für Molekulare Pflanzenphysiologie)
- Alexander Graf
(Max-Planck-Institut für Molekulare Pflanzenphysiologie)
- Lee Sweetlove
(University of Oxford)
- Alisdair R. Fernie
(Max-Planck-Institut für Molekulare Pflanzenphysiologie
Center of Plant Systems Biology and Biotechnology)
Abstract
Glycolysis is one of the primordial pathways of metabolism, playing a pivotal role in energy metabolism and biosynthesis. Glycolytic enzymes are known to form transient multi-enzyme assemblies. Here we examine the wider protein-protein interactions of plant glycolytic enzymes and reveal a moonlighting role for specific glycolytic enzymes in mediating the co-localization of mitochondria and chloroplasts. Knockout mutation of phosphoglycerate mutase or enolase resulted in a significantly reduced association of the two organelles. We provide evidence that phosphoglycerate mutase and enolase form a substrate-channelling metabolon which is part of a larger complex of proteins including pyruvate kinase. These results alongside a range of genetic complementation experiments are discussed in the context of our current understanding of chloroplast-mitochondrial interactions within photosynthetic eukaryotes.
Suggested Citation
Youjun Zhang & Arun Sampathkumar & Sandra Mae-Lin Kerber & Corné Swart & Carsten Hille & Kumar Seerangan & Alexander Graf & Lee Sweetlove & Alisdair R. Fernie, 2020.
"A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts,"
Nature Communications, Nature, vol. 11(1), pages 1-15, December.
Handle:
RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18234-w
DOI: 10.1038/s41467-020-18234-w
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