The mitochondrial complexome of <i>Arabidopsis thaliana</i>

Senkler, Jennifer; Eubel, Holger; Hildebrandt, Tatjana M.; Lengwenus, Christian; Schertl, Peter; Schwarzländer, Markus; Wagner, Stephan; Wittig, Ilka; Braun, Hans‐Peter

doi:10.1111/tpj.13448

Cited by 193 publications

(227 citation statements)

References 69 publications

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“…Some further plant‐specific proteins are discussed to be candidates for additional complex I subunits (Peters et al , Braun et al ). However, their association with complex I could not be confirmed by a recent complexome profiling analysis using a total mitochondrial fraction of A. thaliana (Senkler et al ). These proteins therefore are not included in Table .…”

Section: Comparison Of Plant and Animal Complex Imentioning

confidence: 93%

Structure and function of complex I in animals and plants – a comparative view

Senkler

Braun

2017

Physiologia Plantarum

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The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40-50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms.

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Section: Comparison Of Plant and Animal Complex Imentioning

confidence: 93%

Structure and function of complex I in animals and plants – a comparative view

Senkler

Braun

2017

Physiologia Plantarum

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“…Added onto this is the occurrence of metabolic channeling of citrate and fumarate, but not 2-OG, in plant mitochondria (Zhang et al, 2017), and the fact that most steps in the TCAC can be bypassed by similar nonmitochondrial activities in other cellular locations means that the matrix subcompartment concentrations are unknown. Finally, the existence of alternative respirasomes, where AOX isoforms are associated with alternative NAD(P)H dehydrogenases, suggests subcompartmentalizations of respiration and that local concentrations of substrates may differ significantly from the concentrations in a given compartment (Senkler et al, 2017).…”

Section: Resultsmentioning

confidence: 99%

Alternative Oxidase Isoforms Are Differentially Activated by Tricarboxylic Acid Cycle Intermediates

et al. 2017

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The cyanide-insensitive alternative oxidase (AOX) is a non-proton-pumping ubiquinol oxidase that catalyzes the reduction of oxygen to water and is posttranslationally regulated by redox mechanisms and 2-oxo acids. Arabidopsis (Arabidopsis thaliana) possesses five AOX isoforms (AOX1A-AOX1D and AOX2). AOX1D expression is increased in aox1a knockout mutants from Arabidopsis (especially after restriction of the cytochrome c pathway) but cannot compensate for the lack of AOX1A, suggesting a difference in the regulation of these isoforms. Therefore, we analyzed the different AOX isoenzymes with the aim to identify differences in their posttranslational regulation. Seven tricarboxylic acid cycle intermediates (citrate, isocitrate, 2-oxoglutarate, succinate, fumarate, malate, and oxaloacetate) were tested for their influence on AOX1A, AOX1C, and AOX1D wild-type protein activity using a refined in vitro system. AOX1C is insensitive to all seven organic acids, AOX1A and AOX1D are both activated by 2-oxoglutarate, but only AOX1A is additionally activated by oxaloacetate. Furthermore, AOX isoforms cannot be transformed to mimic one another by substituting the variable cysteine residues at position III in the protein. In summary, we show that AOX isoforms from Arabidopsis are differentially fine-regulated by tricarboxylic acid cycle metabolites (most likely depending on the amino-terminal region around the highly conserved cysteine residues known to be involved in regulation by the 2-oxo acids pyruvate and glyoxylate) and propose that this is the main reason why they cannot functionally compensate for each other.

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“…Recently, the mitochondrial complexome of Arabidopsis was described (Senkler et al ., ). In this work, complex I subunits were mostly detected within complex I and the supercomplex formed by complex I and complex III.…”

Section: Discussionmentioning

confidence: 97%

The assembly pathway of complex I in Arabidopsis thaliana

et al. 2018

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Summary All present‐day mitochondria originate from a single endosymbiotic event that gave rise to the last eukaryotic common ancestor more than a billion years ago. However, to date, many aspects of mitochondrial evolution have remained unresolved. Comparative genomics and proteomics have revealed a complex evolutionary origin for many mitochondrial components. To understand the evolution of the respiratory chain, we have examined both the components and the mechanisms of the assembly pathway of complex I. Complex I represents the first enzyme in the respiratory chain, and complex I deficiencies have dramatic consequences in both animals and plants. The complex is located in the mitochondrial inner membrane and possesses two arms: one embedded in the inner membrane and one protruding in the matrix. Here, we describe the assembly pathway of complex I in the model plant Arabidopsis thaliana. Using a proteomics approach called complexome profiling, we have resolved the different steps in the assembly process in plants. We propose a model for the stepwise assembly of complex I, including every subunit. We then compare this pathway with the corresponding pathway in humans and find that complex I assembly in plants follows a different, and likely ancestral, pathway compared with the one in humans. We show that the main evolutionary changes in complex I structure and assembly in humans occurred at the level of the membrane arm, whereas the matrix arm remained rather conserved.

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The mitochondrial complexome of Arabidopsis thaliana

Cited by 193 publications

References 69 publications

Structure and function of complex I in animals and plants – a comparative view

Structure and function of complex I in animals and plants – a comparative view

Alternative Oxidase Isoforms Are Differentially Activated by Tricarboxylic Acid Cycle Intermediates

The assembly pathway of complex I in Arabidopsis thaliana

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