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J Biol Chem, Vol. 274, Issue 8, 4613-4619, February 19, 1999
From the Department of Microbiologie Medical School, University of
Innsbruck, Fritz-Pregl Str. 3, A-6020 Innsbruck, Austria
A gene encoding a new GATA factor from
Aspergillus nidulans, sreA, was isolated and
characterized. SREA displays homology to two fungal regulators of
siderophore biosynthesis: about 30% overall identity to SRE from
Neurospora crassa and about 50% identity to URBS1 from
Ustilago maydis over a stretch of 200 amino acid residues
containing two GATA-type zinc finger motifs and a cysteine-rich region.
This putative DNA binding domain, expressed as a fusion protein in
Escherichia coli, specifically binds to GATA sequence motifs. Deletion of sreA results in derepression of
L-ornithine-N5-oxygenase activity
and consequently in derepression of the biosynthesis of the hydroxamate
siderophore N,N',N''-triacetyl
fusarinine under sufficient iron supply in A. nidulans.
Transcription of sreA is confined to high iron conditions,
underscoring the function of SREA as a repressor of siderophore
biosynthesis under sufficient iron supply. Nevertheless, overexpression
of sreA does not result in repression of siderophore
synthesis under low iron conditions, suggesting additional mechanisms
involved in this regulatory circuit. Consistent with increased
sensitivity to the iron-activated antibiotics phleomycin and
streptonigrin, the sreA deletion mutant displays increased
accumulation of 59Fe. These results demonstrate that SREA
plays a central role in iron uptake in addition to siderophore biosynthesis.
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