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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.

Original publication




Journal article


Nat Commun

Publication Date





Arabidopsis, Arabidopsis Proteins, Chloroplasts, Energy Metabolism, Glycolysis, Mitochondria, Mutation, Phosphoglycerate Mutase, Phosphopyruvate Hydratase, Photosynthesis, Plants, Genetically Modified, Protein Interaction Mapping, Protein Interaction Maps, Pyruvate Kinase