Dealing with the sulfur part of cysteine: four enzymaticsteps degrade L-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Saskia Höfler
  • Christin Lorenz
  • Tjorven Busch
  • Mascha Brinkkötter
  • Takayuki Tohge
  • Alisdair R. Fernie
  • Hans Peter Braun
  • Tatjana M. Hildebrandt

Organisationseinheiten

Externe Organisationen

  • Max-Planck-Institut für molekulare Pflanzenphysiologie
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)352-366
Seitenumfang15
FachzeitschriftPhysiologia plantarum
Jahrgang157
Ausgabenummer3
PublikationsstatusVeröffentlicht - 23 Apr. 2016

Abstract

Amino acid catabolism is essential for adjusting pool sizes of free amino acids and takes part in energy production as well as nutrient remobilization. The carbon skeletons are generally converted to precursors or intermediates of the tricarboxylic acid cycle. In the case of cysteine, the reduced sulfur derived from the thiol group also has to be oxidized in order to prevent accumulation to toxic concentrations. Here we present a mitochondrial sulfur catabolic pathway catalyzing the complete oxidation of l-cysteine to pyruvate and thiosulfate. After transamination to 3-mercaptopyruvate, the sulfhydryl group from l-cysteine is transferred to glutathione by sulfurtransferase 1 and oxidized to sulfite by the sulfur dioxygenase ETHE1. Sulfite is then converted to thiosulfate by addition of a second persulfide group by sulfurtransferase 1. This pathway is most relevant during early embryo development and for vegetative growth under light-limiting conditions. Characterization of a double mutant produced from Arabidopsis thaliana T-DNA insertion lines for ETHE1 and sulfurtransferase 1 revealed that an intermediate of the ETHE1 dependent pathway, most likely a persulfide, interferes with amino acid catabolism and induces early senescence.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Physiologie
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Zellbiologie

Zitieren

Dealing with the sulfur part of cysteine: four enzymaticsteps degrade L-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria. / Höfler, Saskia; Lorenz, Christin; Busch, Tjorven et al.
in: Physiologia plantarum, Jahrgang 157, Nr. 3, 23.04.2016, S. 352-366.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Höfler S, Lorenz C, Busch T, Brinkkötter M, Tohge T, Fernie AR et al. Dealing with the sulfur part of cysteine: four enzymaticsteps degrade L-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria. Physiologia plantarum. 2016 Apr 23;157(3):352-366. doi: 10.1111/ppl.12454
Höfler, Saskia ; Lorenz, Christin ; Busch, Tjorven et al. / Dealing with the sulfur part of cysteine : four enzymaticsteps degrade L-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria. in: Physiologia plantarum. 2016 ; Jahrgang 157, Nr. 3. S. 352-366.
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abstract = "Amino acid catabolism is essential for adjusting pool sizes of free amino acids and takes part in energy production as well as nutrient remobilization. The carbon skeletons are generally converted to precursors or intermediates of the tricarboxylic acid cycle. In the case of cysteine, the reduced sulfur derived from the thiol group also has to be oxidized in order to prevent accumulation to toxic concentrations. Here we present a mitochondrial sulfur catabolic pathway catalyzing the complete oxidation of l-cysteine to pyruvate and thiosulfate. After transamination to 3-mercaptopyruvate, the sulfhydryl group from l-cysteine is transferred to glutathione by sulfurtransferase 1 and oxidized to sulfite by the sulfur dioxygenase ETHE1. Sulfite is then converted to thiosulfate by addition of a second persulfide group by sulfurtransferase 1. This pathway is most relevant during early embryo development and for vegetative growth under light-limiting conditions. Characterization of a double mutant produced from Arabidopsis thaliana T-DNA insertion lines for ETHE1 and sulfurtransferase 1 revealed that an intermediate of the ETHE1 dependent pathway, most likely a persulfide, interferes with amino acid catabolism and induces early senescence. ",
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AU - Höfler, Saskia

AU - Lorenz, Christin

AU - Busch, Tjorven

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AU - Tohge, Takayuki

AU - Fernie, Alisdair R.

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