A trypanosomatid protein specifically interacts with a mammalian iron-responsive element |
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Authors: | Heather A Meehan Richard A Lundberg Gregory J Connell |
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Institution: | (1) Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455-0347, USA e-mail: gconnell@lenti.med.umn.edu Tel.: +1-612-6243132; Fax: +1-612-6258408, US |
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Abstract: | Intracellular iron homeostasis of vertebrates and invertebrates is mediated through the interaction of iron-regulatory proteins
(IRPs) with mRNAs containing a bulged hairpin-loop structure termed the iron-responsive element (IRE). We detected a protein
within extracts prepared from Leishmania tarentolae that specifically interacts with a mammalian IRE; mutations to the IRE that inhibit the interaction with the mammalian protein
have a corresponding effect on the interaction with the L. tarentolae protein. The disassociation constant noted for the interaction of the mammalian IRE with the L. tarentolae protein was 0.7 ± 0.3 μM, whereas that recorded for the interaction with the mammalian IRP under these conditions was 5 ± 2 nM. The interacting L. tarentolae protein potentially places the RNA-binding site of the IRP near the root of the eukaryotic evolutionary tree. However, unlike
that of the mammalian IRPs, the L. tarentolae IRE-binding activity was not induced by growth in iron-depleted media.
Received: 21 June 1999 / Accepted: 15 September 1999 |
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