Recent evidence suggests an important role for nitric oxide (NO) signaling
in plant-pathogen interactions. Additional elucidation of the role of NO in
plants will require identification of NO targets. Since aconitases are maj
or NO targets in animals, we examined the effect of NO on tobacco (Nicotian
a tabacum) aconitase. The tobacco aconitases, like their animal counterpart
s, were inhibited by NO donors. The cytosolic aconitase in animals, in addi
tion to being a key redox and NO sensor, is converted by NO into an mRNA bi
nding protein (IRP, or iron-regulatory protein) that regulates iron homeost
asis. A tobacco cytosolic aconitase gene (NtACO1) whose deduced amino acid
sequence shared 61% identity and 76% similarity with the human IRP-1 was cl
oned. Furthermore, residues involved in mRNA binding by IRP-1 were conserve
d in NtACO1. These results reveal additional similarities between the NO si
gnaling mechanisms used by plants and animals.