Animal cytosolic ACO (aconitase) and bacteria ACO are able to switch to RNA-binding proteins [IRPs (iron-regulatory proteins)], thereby playing a key role in the regulation of iron homoeostasis. In the model plant Arabidopsis thaliana, we have identified three IRP1 homologues, named ACO1–3. To determine whether or not they may encode functional IRP proteins and regulate iron homoeostasis in plants, we have isolated loss-of-function mutants in the three genes. The aco1-1 and aco3-1 mutants show a clear decrease in cytosolic ACO activity. However, none of the mutants is affected in respect of the accumulation of the ferritin transcript or protein in response to iron excess. cis-acting elements potentially able to bind to the IRP have been searched for in silico in the Arabidopsis genome. They appear to be very rare sequences, found in the 5′-UTR (5′-untranslated region) or 3′-UTR of a few genes unrelated to iron metabolism. They are therefore unlikely to play a functional role in the regulation of iron homoeostasis. Taken together, our results demonstrate that, in plants, the cytosolic ACO is not converted into an IRP and does not regulate iron homoeostasis. In contrast with animals, the RNA binding activity of plant ACO, if any, would be more likely to be attributable to a structural element, rather than to a canonical sequence.
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Research Article|
July 13 2007
The iron-responsive element (IRE)/iron-regulatory protein 1 (IRP1)–cytosolic aconitase iron-regulatory switch does not operate in plants
Nicolas Arnaud;
Nicolas Arnaud
1
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Karl Ravet;
Karl Ravet
1
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Andrea Borlotti;
Andrea Borlotti
2
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Brigitte Touraine;
Brigitte Touraine
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Jossia Boucherez;
Jossia Boucherez
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Cécile Fizames;
Cécile Fizames
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Jean-François Briat;
Jean-François Briat
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Françoise Cellier;
Françoise Cellier
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
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Frédéric Gaymard
Frédéric Gaymard
3
1Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier cedex 1, France
3To whom correspondence should be addressed (email gaymard@supagro.inra.fr).
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Publisher: Portland Press Ltd
Received:
December 15 2006
Revision Received:
March 28 2007
Accepted:
April 16 2007
Accepted Manuscript online:
April 16 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem J (2007) 405 (3): 523–531.
Article history
Received:
December 15 2006
Revision Received:
March 28 2007
Accepted:
April 16 2007
Accepted Manuscript online:
April 16 2007
Citation
Nicolas Arnaud, Karl Ravet, Andrea Borlotti, Brigitte Touraine, Jossia Boucherez, Cécile Fizames, Jean-François Briat, Françoise Cellier, Frédéric Gaymard; The iron-responsive element (IRE)/iron-regulatory protein 1 (IRP1)–cytosolic aconitase iron-regulatory switch does not operate in plants. Biochem J 1 August 2007; 405 (3): 523–531. doi: https://doi.org/10.1042/BJ20061874
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