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


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.

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC7481185 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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

Zhang Youjun Y   Sampathkumar Arun A   Kerber Sandra Mae-Lin SM   Swart Corné C   Hille Carsten C   Seerangan Kumar K   Graf Alexander A   Sweetlove Lee L   Fernie Alisdair R AR  

Nature communications 20200909 1


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 a  ...[more]

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