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Complexome Profiling of Plant Mitochondrial Fractions

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Plant Mitochondria

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2363))

Abstract

Most molecular functions depend on defined associations of proteins. Protein–protein interactions may be transient or long-lasting; they may lead to labile assemblies or more stable particles termed protein complexes. Studying protein–protein interactions is of prime importance for understanding molecular functions in cells. The complexome profiling approach allows to systematically analyze protein assemblies of cells or subcellular compartments. It combines separation of intact protein fractions by blue native (BN) polyacrylamide gel electrophoresis (PAGE) and protein identification as well as quantification by mass spectrometry. Complexome profiling has been successfully applied to characterize mitochondrial fractions of plants. In a typical experiment, more than 1000 mitochondrial proteins are identified and assigned to defined protein assemblies. It allows discovering so far unknown protein complexes, studying assembly pathways of protein complexes and even characterizing labile super- and megacomplexes in the >10 mega-Dalton range. We here present a complexome profiling protocol for the straightforward definition of the protein complex inventory of mitochondria or other subcellular compartments from plants.

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Correspondence to Holger Eubel or Hans-Peter Braun .

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Schröder, L., Eubel, H., Braun, HP. (2022). Complexome Profiling of Plant Mitochondrial Fractions. In: Van Aken, O., Rasmusson, A.G. (eds) Plant Mitochondria. Methods in Molecular Biology, vol 2363. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1653-6_9

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  • DOI: https://doi.org/10.1007/978-1-0716-1653-6_9

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1652-9

  • Online ISBN: 978-1-0716-1653-6

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