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J Biol Chem, Vol. 274, Issue 1, 516-521, January 1, 1999
From the Institut de Chimie des Substances Naturelles, CNRS,
Avenue de la Terrasse, 91190 Gif-sur-Yvette, France
Iron regulatory proteins (IRP1 and IRP2) are
redox-sensitive RNA-binding proteins that modulate the expression of
several genes encoding key proteins of iron metabolism. IRP1 can also exist as an aconitase containing a [4Fe-4S] cluster bound to three cysteines at the active site. We previously showed that biosynthesis of
nitric oxide (NO) induces the transition of IRP1 from aconitase to
apoprotein able to bind RNA. This switch is also observed when cytosolic extracts are exposed to NO donors. However, the activation of
IRP1 under these conditions is far from maximal. In this study we
examined the capacity of physiological reducing systems to cooperate
with NO in the activation of IRP1. Cytosolic extracts from the
macrophage cell line RAW 264.7 or purified IRP1 were incubated with NO
donors and subsequently exposed to glutathione or to thioredoxin (Trx),
a strong protein disulfide reductase. Trx was the most effective,
inducing a 2-6-fold enhancement of the RNA binding activity of
NO-treated IRP1. Furthermore, the effect of NO on IRP1 from cytosolic
extracts was abolished in the presence of anti-Trx antibodies. We also
studied the combined effect of NO and Trx on IRP2, which exhibits
constitutive RNA binding activity. We observed an inhibition of IRP2
activity following exposure to NO donors which was restored by Trx.
Collectively, these results point to a crucial role of Trx as a
modulator of IRP activity in situations of NO production.
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