Fuchs, Philippe, Rugen, Nils ORCID: 0000-0002-9297-4560, Carrie, Chris ORCID: 0000-0002-4240-4674, Elsaesser, Marlene, Finkemeier, Iris ORCID: 0000-0002-8972-4026, Giese, Jonas ORCID: 0000-0001-5970-1037, Hildebrandt, Tatjana M., Kuehn, Kristina ORCID: 0000-0001-6747-783X, Maurino, Veronica G., Ruberti, Cristina ORCID: 0000-0002-9013-1412, Schallenberg-Ruedinger, Mareike, Steinbeck, Janina, Braun, Hans-Peter ORCID: 0000-0002-4459-9727, Eubel, Holger, Meyer, Etienne H., Mueller-Schuessele, Stefanie J. and Schwarzlaender, Markus (2020). Single organelle function and organization as estimated from Arabidopsis mitochondrial proteomics. Plant J., 101 (2). S. 420 - 442. HOBOKEN: WILEY. ISSN 1365-313X

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Abstract

Mitochondria host vital cellular functions, including oxidative phosphorylation and co-factor biosynthesis, which are reflected in their proteome. At the cellular level plant mitochondria are organized into hundreds of discrete functional entities, which undergo dynamic fission and fusion. It is the individual organelle that operates in the living cell, yet biochemical and physiological assessments have exclusively focused on the characteristics of large populations of mitochondria. Here, we explore the protein composition of an individual average plant mitochondrion to deduce principles of functional and structural organisation. We perform proteomics on purified mitochondria from cultured heterotrophic Arabidopsis cells with intensity-based absolute quantification and scale the dataset to the single organelle based on criteria that are justified by experimental evidence and theoretical considerations. We estimate that a total of 1.4 million protein molecules make up a single Arabidopsis mitochondrion on average. Copy numbers of the individual proteins span five orders of magnitude, ranging from >40 000 for Voltage-Dependent Anion Channel 1 to sub-stoichiometric copy numbers, i.e. less than a single copy per single mitochondrion, for several pentatricopeptide repeat proteins that modify mitochondrial transcripts. For our analysis, we consider the physical and chemical constraints of the single organelle and discuss prominent features of mitochondrial architecture, protein biogenesis, oxidative phosphorylation, metabolism, antioxidant defence, genome maintenance, gene expression, and dynamics. While assessing the limitations of our considerations, we exemplify how our understanding of biochemical function and structural organization of plant mitochondria can be connected in order to obtain global and specific insights into how organelles work.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Fuchs, PhilippeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Rugen, NilsUNSPECIFIEDorcid.org/0000-0002-9297-4560UNSPECIFIED
Carrie, ChrisUNSPECIFIEDorcid.org/0000-0002-4240-4674UNSPECIFIED
Elsaesser, MarleneUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Finkemeier, IrisUNSPECIFIEDorcid.org/0000-0002-8972-4026UNSPECIFIED
Giese, JonasUNSPECIFIEDorcid.org/0000-0001-5970-1037UNSPECIFIED
Hildebrandt, Tatjana M.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Kuehn, KristinaUNSPECIFIEDorcid.org/0000-0001-6747-783XUNSPECIFIED
Maurino, Veronica G.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Ruberti, CristinaUNSPECIFIEDorcid.org/0000-0002-9013-1412UNSPECIFIED
Schallenberg-Ruedinger, MareikeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Steinbeck, JaninaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Braun, Hans-PeterUNSPECIFIEDorcid.org/0000-0002-4459-9727UNSPECIFIED
Eubel, HolgerUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Meyer, Etienne H.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Mueller-Schuessele, Stefanie J.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Schwarzlaender, MarkusUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-128254
DOI: 10.1111/tpj.14534
Journal or Publication Title: Plant J.
Volume: 101
Number: 2
Page Range: S. 420 - 442
Date: 2020
Publisher: WILEY
Place of Publication: HOBOKEN
ISSN: 1365-313X
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
PENTATRICOPEPTIDE REPEAT PROTEINS; GLYCINE DECARBOXYLASE; PLANT-MITOCHONDRIA; COMPLEX-I; FERROCHELATASE-I; INNER MEMBRANE; RAT-LIVER; DIHYDROLIPOAMIDE DEHYDROGENASE; SUPERRESOLUTION MICROSCOPY; SUBCELLULAR-LOCALIZATIONMultiple languages
Plant SciencesMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/12825

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