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J. Biol. Chem., Vol. 277, Issue 34, 31220-31227, August 23, 2002
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From the Institut de Chimie des Substances Naturelles, CNRS, Avenue
de la Terrasse, 91190 Gif-sur-Yvette, France
Iron regulatory proteins (IRPs) control iron
metabolism by specifically interacting with iron-responsive elements
(IREs) on mRNAs. Nitric oxide (NO) converts IRP-1 from a [4Fe-4S]
aconitase to a trans-regulatory protein through Fe-S
cluster disassembly. Here, we have focused on the fate of IRE binding
IRP1 from murine macrophages when NO flux stops. We show that virtually
all IRP-1 molecules from NO-producing cells dissociated from IRE and
recovered aconitase activity after re-assembling a [4Fe-4S] cluster
in vitro. The reverse change in IRP-1 activities also
occurred in intact cells no longer exposed to NO and did not require
de novo protein synthesis. Likewise, inhibition of
mitochondrial aconitase via NO-induced Fe-S cluster disassembly was
also reversed independently of protein translation after NO removal.
Our results provide the first evidence of Fe-S cluster repair of
NO-modified aconitases in mammalian cells. Moreover, we show that
reverse change in IRP-1 activities and repair of mitochondrial
aconitase activity depended on energized mitochondria. Finally, we
demonstrate that IRP-1 activation by NO was accompanied by both a
drastic decrease in ferritin levels and an increase in transferrin
receptor mRNA levels. However, although ferritin expression was
recovered upon IRP-1-IRE dissociation, expression of transferrin
receptor mRNA continued to rise for several hours after stopping NO flux.
Recycling of RNA Binding Iron Regulatory Protein 1 into an
Aconitase after Nitric Oxide Removal Depends on Mitochondrial
ATP*
*
This work was supported in part by Association pour la
Recherche contre le Cancer Grant 5856.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
33-1-69-82-45-62; Fax: 33-1-69-07-72-47; E-mail:
Jean-Claude.Drapier@icsn.cnrs-gif.fr.
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