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- W2616118570 abstract "Protein complexes of sequential metabolic enzymes, often termed metabolons, may permit direct channelling of metabolites between the enzymes, providing increased control over metabolic pathway fluxes. Experimental evidence supporting their existence in vivo remains fragmentary. In the present study, we test binary interactions of the proteins constituting the plant tricarboxylic acid (TCA) cycle. We integrate (semi-)quantitative results from affinity purification-mass spectrometry, split-luciferase and yeast-two-hybrid assays to generate a single reliability score for assessing protein-protein interactions. By this approach, we identify 158 interactions including those between catalytic subunits of sequential enzymes and between subunits of enzymes mediating non-adjacent reactions. We reveal channelling of citrate and fumarate in isolated potato mitochondria by isotope dilution experiments. These results provide evidence for a functional TCA cycle metabolon in plants, which we discuss in the context of contemporary understanding of this pathway in other kingdoms." @default.
- W2616118570 created "2017-05-26" @default.
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- W2616118570 date "2017-05-16" @default.
- W2616118570 modified "2023-10-12" @default.
- W2616118570 title "Protein-protein interactions and metabolite channelling in the plant tricarboxylic acid cycle" @default.
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- W2616118570 doi "https://doi.org/10.1038/ncomms15212" @default.
- W2616118570 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5440813" @default.
- W2616118570 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28508886" @default.
- W2616118570 hasPublicationYear "2017" @default.