Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex

Fromm, Steffanie; Senkler, Jennifer; Eubel, Holger; Peterhänsel, Christoph; Braun, Hans‐Peter

doi:10.1093/jxb/erw165

Cited by 96 publications

(75 citation statements)

References 81 publications

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“…Their presence has implications for the physiological role of complex I. However, even in plants, complex I is an essential site for electron flow into the ETC under most physiological conditions, as deletion of complex I genes causes a drastic delay in plant development and loss of plant fertility (Fromm et al ).…”

Section: Mitochondrial Complex I From Plantsmentioning

confidence: 99%

“…Simultaneous deletion of two of the genes encoding CA/CAL proteins caused strong developmental problems at the seed stage (CAL1 + CAL2 deletion or CA1 + CA2 deletion), except if one of the two deleted genes encoded CA3 (e.g. CA1 + CA3 deletion) (Wang et al , Córdoba et al , Fromm et al , ). Seeds from CA1/CA2 double‐mutant could be rescued by cultivation on sucrose; plants could be regenerated, but were strongly delayed in development (Fromm et al ).…”

Section: Mitochondrial Complex I From Plantsmentioning

confidence: 99%

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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: Mitochondrial Complex I From Plantsmentioning

confidence: 99%

Section: Mitochondrial Complex I From Plantsmentioning

confidence: 99%

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

Senkler

Braun

2017

Physiologia Plantarum

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“…The γca1γca2 mutants lack Complex I altogether, and do not produce viable seed, having to be maintained using an embryo rescue method, which involves supplying the embryos with sucrose in the growth medium (Fromm et al., 2016a, Fromm et al., 2016b). The double mutants also exhibit high levels of Complexes II and IV (succinate dehydrogenase and cytochrome oxidase, respectively), and the alternative oxidase, and in contrast, reduced levels of photosynthetic proteins (Fromm et al., 2016c). …”

Section: Plant γ Carbonic Anhydrasesmentioning

confidence: 99%

Plant Carbonic Anhydrases: Structures, Locations, Evolution, and Physiological Roles

et al. 2017

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Carbonic anhydrases (CAs) are zinc metalloenzymes that catalyze the interconversion of CO2 and HCO3− and are ubiquitous in nature. Higher plants contain three evolutionarily distinct CA families, αCAs, βCAs, and γCAs, where each family is represented by multiple isoforms in all species. Alternative splicing of CA transcripts appears common; consequently, the number of functional CA isoforms in a species may exceed the number of genes. CAs are expressed in numerous plant tissues and in different cellular locations. The most prevalent CAs are those in the chloroplast, cytosol, and mitochondria. This diversity in location is paralleled in the many physiological and biochemical roles that CAs play in plants. In this review, the number and types of CAs in C3, C4, and crassulacean acid metabolism (CAM) plants are considered, and the roles of the α and γCAs are briefly discussed. The remainder of the review focuses on plant βCAs and includes the identification of homologs between species using phylogenetic approaches, a consideration of the inter- and intracellular localization of the proteins, along with the evidence for alternative splice forms. Current understanding of βCA tissue-specific expression patterns and what controls them are reviewed, and the physiological roles for which βCAs have been implicated are presented.

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“…In contrast, Complex I is responsible for oxidation of NADH produced during respiration and it is the main point of entry of electrons into the mitochondrial electron transfer chain, providing up to 40% of the protons for the formation of ATP (Fromm et al ). Unlike its chloroplast counterpart, lack of this complex affects carbon metabolism and photosynthesis (Fromm et al ), and entails profound changes leading to curled leaves and delayed reproductive and vegetative development phenotype (de Longevialle et al ). Surprisingly, recent studies have found that hemiparasitic mistletoe has lost the ability to produce a functional Complex I (da Fonseca‐Pereira et al ) pointing to more similarities to the NDH complex.…”

Section: Nadh Dehydrogenase: the Main Target?mentioning

confidence: 99%

PPR proteins – orchestrators of organelle RNA metabolism

Rovira

Smith

2019

Physiologia Plantarum

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Pentatricopeptide repeat (PPR) proteins are important RNA regulators in chloroplasts and mitochondria, aiding in RNA editing, maturation, stabilisation or intron splicing, and in transcription and translation of organellar genes. In this review, we summarise all PPR proteins documented so far in plants and the green alga Chlamydomonas. By further analysis of the known target RNAs from Arabidopsis thaliana PPR proteins, we find that all organellar‐encoded complexes are regulated by these proteins, although to differing extents. In particular, the orthologous complexes of NADH dehydrogenase (Complex I) in the mitochondria and NADH dehydrogenase‐like (NDH) complex in the chloroplast were the most regulated, with respectively 60 and 28% of all characterised A. thaliana PPR proteins targeting their genes.

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Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex

Abstract: HighlightComplex I dysfunction causes reorganization of cellular respiration and affects metabolic processes in mitochondria, plastids, peroxisomes, and other cellular compartments with drastic consequences for growth and development.

Cited by 96 publications

References 81 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

Plant Carbonic Anhydrases: Structures, Locations, Evolution, and Physiological Roles

PPR proteins – orchestrators of organelle RNA metabolism

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