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Originally published In Press as doi:10.1074/jbc.M602135200 on June 16, 2006
J. Biol. Chem., Vol. 281, Issue 33, 23579-23588, August 18, 2006
An Iron-induced Nitric Oxide Burst Precedes Ubiquitin-dependent Protein Degradation for Arabidopsis AtFer1 Ferritin Gene Expression*
Nicolas Arnaud 1,
Irene Murgia ,
Jossia Boucherez ,
Jean-François Briat ,
Françoise Cellier , and
Frédéric Gaymard 2
From the
Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 Agro-M/CNRS/INRA/UMII, Bat 7, 2 place Viala, 34060 Montpellier Cedex 1, France and the Sezione di Fisiologia e Biochimica delle Piante, Dipartimento di Biologia, Università degli Studi di Milano, via Celoria 26, 20133 Milano, Italy
Ferritins play an essential role in iron homeostasis by sequestering iron in a bioavailable and non-toxic form. In plants, ferritin mRNAs are highly and quickly accumulated in response to iron overload. Such accumulation leads to a subsequent ferritin protein synthesis and iron storage, thus avoiding oxidative stress to take place. By combining pharmacological and imaging approaches in an Arabidopsis cell culture system, we have identified several elements in the signal transduction pathway leading to the increase of AtFer1 transcript level after iron treatment. Nitric oxide quickly accumulates in the plastids after iron treatment. This compound acts downstream of iron and upstream of a PP2A-type phosphatase to promote an increase of AtFer1 mRNA level. The AtFer1 gene transcription has been previously shown to be repressed under low iron conditions with the involvement of the cis-acting element iron-dependent regulatory sequence identified within the AtFer1 promoter sequence. We show here that the repressor is unlikely a transcription factor directly bound to the iron-dependent regulatory sequence; such a repressor is ubiquitinated upon iron treatment and subsequently degraded through a 26 S proteasome-dependent pathway.
Received for publication, March 7, 2006
, and in revised form, May 2, 2006.
* This work was supported by Institut National de la Recherche Agronomique and Centre National de la Recherche Scientifique, Action Concertée Incitative "Biologie Cellulaire Moléculaire et Structurale" Grant BCMS166 from the Ministère de l'Education Nationale, de l'Enseignement Supérieur et de la Recherche. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 Supported by a thesis fellowship from the Ministère de l'Education Nationale, de l'Enseignement Supérieur et de la Recherche.
2 To whom correspondence should be addressed. Tel.: 33-499-61-29-32; Fax: 33-467-52-57-37; E-mail: gaymard{at}ensam.inra.fr.

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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