The Mitochondrial Sulfur Dioxygenase ETHYLMALONIC ENCEPHALOPATHY PROTEIN1 Is Required for Amino Acid Catabolism during Carbohydrate Starvation and Embryo Development in Arabidopsis

Krüßel, Lena; Junemann, Johannes; Wirtz, Markus; Birke, Hannah; Thornton, Jeremy; Browning, Luke W.; Poschet, Gernot; Hell, Rüdiger; Balk, Janneke; Braun, Hans‐Peter; Hildebrandt, Tatjana M.

doi:10.1104/pp.114.239764

Cited by 53 publications

(63 citation statements)

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“…Sulfite oxidase, present in the intermitochondrial membrane space, oxidizes sulfite to sulfate. Organization of the sulfide oxidation pathway can vary in different archaea, bacteria and plants, variously including components that are homologous to the mammalian enzymes or different from them 73–75 .…”

Section: Mitochondrial H2s Oxidation Pathway: a Source Of Rss?mentioning

confidence: 99%

Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways

2015

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The chemical species involved in H2S signaling remain elusive despite the profound and pleiotropic physiological effects elicited by this molecule. The dominant candidate mechanism for sulfide signaling is persulfidation of target proteins. However, the relatively poor reactivity of H2S toward oxidized thiols, such as disulfides, the low concentration of disulfides in the reducing milieu of the cell and the low steady-state concentration of H2S raise questions about the plausibility of persulfide formation via reaction between an oxidized thiol and a sulfide anion or a reduced thiol and oxidized hydrogen disulfide. In contrast, sulfide oxidation pathways, considered to be primarily mechanisms for disposing of excess sulfide, generate a series of reactive sulfur species, including persulfides, polysulfides and thiosulfate, that could modify target proteins. We posit that sulfide oxidation pathways mediate sulfide signaling and that sulfurtransferases ensure target specificity.

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Section: Mitochondrial H2s Oxidation Pathway: a Source Of Rss?mentioning

confidence: 99%

Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways

2015

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“…To provide physiological evidence that a glutathione persulfide may be transported by ATM3 in the model plant Arabidopsis, atm3 mutations were combined with a non-lethal mutant allele of ETHE1, encoding a matrix-located sulfur dioxygenase. The ethylmalonic encephalopathy protein ETHE1 in humans and plants ETHE1 detoxifies persulfide using glutathione as a cofactor [46,47]. Most of the double atm3 ethe1 mutants died during embryogenesis, indicating that toxic persulfide accumulates in the mitochondrial matrix when ATM3 is not functional [13].…”

Section: Abcb7 and Its Homologues In Different Eukaryotesmentioning

confidence: 99%

Structures and functions of mitochondrial ABC transporters

Schaedler

Faust

Shintre

et al. 2015

Biochemical Society Transactions

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A small number of physiologically important ATP-binding cassette (ABC) transporters are found in mitochondria. Most are half transporters of the B group forming homodimers and their topology suggests they function as exporters. The results of mutant studies point towards involvement in iron cofactor biosynthesis. In particular, ABC subfamily B member 7 (ABCB7) and its homologues in yeast and plants are required for iron-sulfur (Fe-S) cluster biosynthesis outside of the mitochondria, whereas ABCB10 is involved in haem biosynthesis. They also play a role in preventing oxidative stress. Mutations in ABCB6 and ABCB7 have been linked to human disease. Recent crystal structures of yeast Atm1 and human ABCB10 have been key to identifying substrate-binding sites and transport mechanisms. Combined with in vitro and in vivo studies, progress is being made to find the physiological substrates of the different mitochondrial ABC transporters. Sequence analysis of mitochondrial ABC transportersMitochondria of most eukaryote species harbour 2-4 different ABC transporters that belong to the B subfamily of half transporters. The proteins contain an N-terminal transmembrane domain (TMD) and a C-terminal nucleotidebinding domain (NBD), which form homodimers for full functionality [1]. Plant and algal genomes additionally encode a unique ABC transporter, termed cytochrome c maturation (Ccm)AB, in which the TMD and NBD are encoded by separate genes. CcmAB is placed in the ABCI subfamily, see section 'CcmAB in plant mitochondria'. Phylogenetic relationship of mitochondrial transporters of the ABCB subfamilyAs a starting point for the discussion of recent crystal structures and functional data, we have reanalysed the phylogenetic relationships of B-type mitochondrial ABC transporters and their closest prokaryotic homologues (Figure 1). The CcmAB proteins were excluded from the phylogenetic analysis due to their large evolutionary distance from the other mitochondrial ABC transporters.Key words: ATP-binding cassette (ABC) transporter, glutathione, haem, iron, mitochondria, oxidative stress. Abbreviations: ABC, ATP-binding cassette; Aft, Activator of ferrous transport; ATM, ABC transporter of the mitochondria; Ccm, cytochrome c maturation; dALA, δ-amino levulinic acid; IRP1, iron regulatory protein 1; Mdl, multi-drug resistance-like; Mfrn, mitoferrin; NBD, nt-binding domain; PPIX, protoporphyrin IX; TMD, transmembrane domain; TMH, transmembrane helix. 1 To whom correspondence should be addressed (email janneke.balk@jic.ac.uk).The ABCB7 group, which includes the ABC transporters of the mitochondria Atm1 in yeast and ATM3 in Arabidopsis, can be found in virtually all eukaryotic species. Human ABCB7 and Arabidopsis ATM3 can largely rescue the phenotypes of yeast atm1 mutants [2][3][4], providing experimental support that members of this subfamily may have the same function. Human ABCB6 can also partially complement a yeast atm1 mutant [5] but differences in the intracellular localization of ABCB6 and Atm1 may point to distinct phys...

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“…In contrast, in Arabidopsis extended darkness has been reported to induce AtETHE1 expression where it is involved in protein turnover processes. 2 Collectively, light has a pronounced effect on stress response of OsETHE1 in both roots and shoots, much like the sulfur assimilation pathway leading to H 2 S emission which is highly dependent on photosynthetic electron transport, with reduced H 2 S emission in dark except when L-cysteine is supplied. 10 However, in roots, dependence of stress response on light still remains unexplained which can possibly occur through transmission of light signals from shoots to roots.…”

Section: Ethylmalonicmentioning

confidence: 99%

“…4 In Arabidopsis thaliana, ETHE1 has been shown to be critical for seed development 1 and other conditions that involve high protein turnover, and is also involved in the use of amino acids as alternative respiratory substrates. 2 Being part of the mitochondrial sulfur catabolic pathway, AtETHE1 is upregulated in conditions that stimulate nutrient remobilization, such as prolonged darkness, drought, abscisic acid, germination or unfavorable conditions leading to carbohydrate starvation.…”

Section: Ethylmalonicmentioning

confidence: 99%

“…1,2 Being present in a wide range of organisms, including bacteria, plants and humans; ETHE1 is believed to be an important candidate involved in sulfur metabolism. In humans, mutations in ETHE1 lead to a fatal metabolic disease ethylmalonic encephalopathy 3 , which is characterized by an increase in sulfide concentration in the bloodstream, severely damaging vascular endothelium and thus causing main symptoms of the disease.…”

Section: Ethylmalonicmentioning

confidence: 99%

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