A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts

Youjun Zhang (), Arun Sampathkumar, Sandra Mae-Lin Kerber, Corné Swart, Carsten Hille, Kumar Seerangan, Alexander Graf, Lee Sweetlove and Alisdair R. Fernie ()
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Youjun Zhang: Max-Planck-Institut für Molekulare Pflanzenphysiologie
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
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

Nature Communications, 2020, vol. 11, issue 1, 1-15

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-18234-w

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