A trypanosomatid protein specifically interacts with a mammalian iron-responsive element

Heather A. Meehan, Richard A. Lundberg, Gregory J. Connell

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)109-114
Number of pages6
JournalParasitology Research
Volume86
Issue number2
DOIs
StatePublished - Jan 1 2000

Fingerprint Dive into the research topics of 'A trypanosomatid protein specifically interacts with a mammalian iron-responsive element'. Together they form a unique fingerprint.

Cite this