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A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts
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A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts
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Journal Article
A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts
2020
Overview
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.
Protein-protein interactions are thought to channel substrates between consecutive enzymes during glycolysis. Here the authors show that
Arabidopsis
phosphoglycerate mutase and enolase can form a substrate-channelling metabolon and also play a moonlighting role in promoting colocalization of chloroplasts and mitochondria.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/33
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Energy Metabolism - physiology
/ Enzymes
/ Humanities and Social Sciences
/ Mutation
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ Phosphopyruvate Hydratase - genetics
/ Phosphopyruvate Hydratase - metabolism
/ Plants, Genetically Modified
/ Protein Interaction Maps - physiology
/ Proteins
/ Pyruvate Kinase - metabolism
/ Science
