The metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial LIPOAMIDE DEHYDROGENASE2, a key enzyme in oxidative metabolism

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Abstract

Mitochondrial lipoamide dehydrogenase is essential for the activity of four mitochondrial enzyme complexes central to oxidative metabolism. The reduction in protein amount and enzyme activity caused by disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 enhanced the arsenic sensitivity of Arabidopsis thaliana. Both arsenate and arsenite inhibited root elongation, decreased seedling size and increased anthocyanin production more profoundly in knockout mutants than in wild-type seedlings. Arsenate also stimulated lateral root formation in the mutants. The activity of lipoamide dehydrogenase in isolated mitochondria was sensitive to arsenite, but not arsenate, indicating that arsenite could be the mediator of the observed phenotypes. Steady-state metabolite abundances were only mildly affected by mutation of mitochondrial LIPOAMIDE DEHYDROGENASE2. In contrast, arsenate induced the remodelling of metabolite pools associated with oxidative metabolism in wild-type seedlings, an effect that was enhanced in the mutant, especially around the enzyme complexes containing mitochondrial lipoamide dehydrogenase. These results indicate that mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis. Arsenic is a common environmental toxin, but its mode of action is not clear in plants. The disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 increased the sensitivity of Arabidopsis thaliana to arsenate, probably through a mechanism requiring the in planta reduction of arsenate to arsenite. Arsenate induced the remodelling of metabolite pools associated with oxidative metabolism, an effect that was enhanced in the mutant, giving us new clues about the effects of arsenic on Arabidopsis thaliana.

LanguageEnglish
Pages684-695
Number of pages12
JournalPlant, Cell & Environment
Volume37
Issue number3
Early online date11 Nov 2013
DOIs
StatePublished - Mar 2014

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arsenates
Acclimatization
aerobiosis
Arabidopsis
acclimation
Arabidopsis thaliana
Dihydrolipoamide Dehydrogenase
arsenites
Enzymes
enzymes
Arsenic
arsenic
Seedlings
metabolites
mutants
seedlings
knockout mutants
Anthocyanins
arsenic acid
Plantae

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@article{be6b80c0232f417d832a00d1e74121f9,
title = "The metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial LIPOAMIDE DEHYDROGENASE2, a key enzyme in oxidative metabolism",
abstract = "Mitochondrial lipoamide dehydrogenase is essential for the activity of four mitochondrial enzyme complexes central to oxidative metabolism. The reduction in protein amount and enzyme activity caused by disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 enhanced the arsenic sensitivity of Arabidopsis thaliana. Both arsenate and arsenite inhibited root elongation, decreased seedling size and increased anthocyanin production more profoundly in knockout mutants than in wild-type seedlings. Arsenate also stimulated lateral root formation in the mutants. The activity of lipoamide dehydrogenase in isolated mitochondria was sensitive to arsenite, but not arsenate, indicating that arsenite could be the mediator of the observed phenotypes. Steady-state metabolite abundances were only mildly affected by mutation of mitochondrial LIPOAMIDE DEHYDROGENASE2. In contrast, arsenate induced the remodelling of metabolite pools associated with oxidative metabolism in wild-type seedlings, an effect that was enhanced in the mutant, especially around the enzyme complexes containing mitochondrial lipoamide dehydrogenase. These results indicate that mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis. Arsenic is a common environmental toxin, but its mode of action is not clear in plants. The disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 increased the sensitivity of Arabidopsis thaliana to arsenate, probably through a mechanism requiring the in planta reduction of arsenate to arsenite. Arsenate induced the remodelling of metabolite pools associated with oxidative metabolism, an effect that was enhanced in the mutant, giving us new clues about the effects of arsenic on Arabidopsis thaliana.",
keywords = "2-oxoglutarate dehydrogenase, Glycine decarboxylase, Mitochondrial metabolism, Pyruvate dehydrogenase, Stress response",
author = "Weihua Chen and Taylor, {Nicolas L.} and Yingjun Chi and Millar, {A. Harvey} and Hans Lambers and Finnegan, {Patrick M.}",
year = "2014",
month = "3",
doi = "10.1111/pce.12187",
language = "English",
volume = "37",
pages = "684--695",
journal = "Plant, Cell & Environment",
issn = "0140-7791",
publisher = "John Wiley & Sons",
number = "3",

}

TY - JOUR

T1 - The metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial LIPOAMIDE DEHYDROGENASE2, a key enzyme in oxidative metabolism

AU - Chen,Weihua

AU - Taylor,Nicolas L.

AU - Chi,Yingjun

AU - Millar,A. Harvey

AU - Lambers,Hans

AU - Finnegan,Patrick M.

PY - 2014/3

Y1 - 2014/3

N2 - Mitochondrial lipoamide dehydrogenase is essential for the activity of four mitochondrial enzyme complexes central to oxidative metabolism. The reduction in protein amount and enzyme activity caused by disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 enhanced the arsenic sensitivity of Arabidopsis thaliana. Both arsenate and arsenite inhibited root elongation, decreased seedling size and increased anthocyanin production more profoundly in knockout mutants than in wild-type seedlings. Arsenate also stimulated lateral root formation in the mutants. The activity of lipoamide dehydrogenase in isolated mitochondria was sensitive to arsenite, but not arsenate, indicating that arsenite could be the mediator of the observed phenotypes. Steady-state metabolite abundances were only mildly affected by mutation of mitochondrial LIPOAMIDE DEHYDROGENASE2. In contrast, arsenate induced the remodelling of metabolite pools associated with oxidative metabolism in wild-type seedlings, an effect that was enhanced in the mutant, especially around the enzyme complexes containing mitochondrial lipoamide dehydrogenase. These results indicate that mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis. Arsenic is a common environmental toxin, but its mode of action is not clear in plants. The disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 increased the sensitivity of Arabidopsis thaliana to arsenate, probably through a mechanism requiring the in planta reduction of arsenate to arsenite. Arsenate induced the remodelling of metabolite pools associated with oxidative metabolism, an effect that was enhanced in the mutant, giving us new clues about the effects of arsenic on Arabidopsis thaliana.

AB - Mitochondrial lipoamide dehydrogenase is essential for the activity of four mitochondrial enzyme complexes central to oxidative metabolism. The reduction in protein amount and enzyme activity caused by disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 enhanced the arsenic sensitivity of Arabidopsis thaliana. Both arsenate and arsenite inhibited root elongation, decreased seedling size and increased anthocyanin production more profoundly in knockout mutants than in wild-type seedlings. Arsenate also stimulated lateral root formation in the mutants. The activity of lipoamide dehydrogenase in isolated mitochondria was sensitive to arsenite, but not arsenate, indicating that arsenite could be the mediator of the observed phenotypes. Steady-state metabolite abundances were only mildly affected by mutation of mitochondrial LIPOAMIDE DEHYDROGENASE2. In contrast, arsenate induced the remodelling of metabolite pools associated with oxidative metabolism in wild-type seedlings, an effect that was enhanced in the mutant, especially around the enzyme complexes containing mitochondrial lipoamide dehydrogenase. These results indicate that mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis. Arsenic is a common environmental toxin, but its mode of action is not clear in plants. The disruption of mitochondrial LIPOAMIDE DEHYDROGENASE2 increased the sensitivity of Arabidopsis thaliana to arsenate, probably through a mechanism requiring the in planta reduction of arsenate to arsenite. Arsenate induced the remodelling of metabolite pools associated with oxidative metabolism, an effect that was enhanced in the mutant, giving us new clues about the effects of arsenic on Arabidopsis thaliana.

KW - 2-oxoglutarate dehydrogenase

KW - Glycine decarboxylase

KW - Mitochondrial metabolism

KW - Pyruvate dehydrogenase

KW - Stress response

U2 - 10.1111/pce.12187

DO - 10.1111/pce.12187

M3 - Article

VL - 37

SP - 684

EP - 695

JO - Plant, Cell & Environment

T2 - Plant, Cell & Environment

JF - Plant, Cell & Environment

SN - 0140-7791

IS - 3

ER -