@article{ZhangSampathkumarKerberetal.2020, author = {Zhang, Youjun and Sampathkumar, Arun and Kerber, Sandra Mae-Lin and Swart, Corn{\´e} and Hille, Carsten and Seerangan, Kumar and Graf, Alexander and Sweetlove, Lee and Fernie, Alisdair R.}, title = {A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts}, series = {Nature Communications}, volume = {11}, journal = {Nature Communications}, issn = {2041-1723}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-14812}, pages = {4509}, year = {2020}, 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.}, language = {en} }