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Plant Physiol, February 2000, Vol. 122, pp. 573-582
Nitric Oxide Modulates the Activity of Tobacco
Aconitase1
Duroy A.
Navarre,
David
Wendehenne,2
Jörg
Durner,3
Robert
Noad, and
Daniel F.
Klessig*
Waksman Institute and Department of Molecular Biology and
Biochemistry, Rutgers, the State University of New Jersey, 190 Frelinghuysen Road, Piscataway, New Jersey 08854-8020.
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 major NO targets in animals, we examined the effect of NO on
tobacco (Nicotiana tabacum) aconitase. The tobacco
aconitases, like their animal counterparts, were inhibited by NO
donors. The cytosolic aconitase in animals, in addition to being a key
redox and NO sensor, is converted by NO into an mRNA binding protein
(IRP, or iron-regulatory protein) that regulates iron homeostasis. A
tobacco cytosolic aconitase gene (NtACO1) whose deduced
amino acid sequence shared 61% identity and 76% similarity with the
human IRP-1 was cloned. Furthermore, residues involved in mRNA binding
by IRP-1 were conserved in NtACO1. These results reveal additional
similarities between the NO signaling mechanisms used by plants and animals.
1
This work was supported by the National Science
Foundation (grant nos. MCB 9723952 and MCB 9514239).
2
Present address: Unité associée
Institut National de la Recherche Agronomique/Université de
Bourgogne, Institut National de la Recherche Agronomique AV 1540, 21034 Dijon cedex, France.
3
Present address: Institute of Biochemical Plant
Pathology, GSF-National Research Center for Environment & Health, D-85764, Oberschleissheim, Germany.
*
Corresponding author; e-mail klessig{at}waksman.rutgers.edu; fax
732-445-5735.
© 2000 American Society of Plant Physiologists
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