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PMID: 12487628 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterization of the Aspergillus nidulans transporters for the siderophores enterobactin and triacetylfusarinine C.

The Biochemical journal ·Vol. 371 ·No. Pt 2 ·2003-04-15 ·Pages 505-13

Haas H, Schoeser M, Lesuisse E, Ernst JF, Parson W, Abt B, Winkelmann G, Oberegger H

Abstract

The filamentous ascomycete Aspergillus nidulans produces three major siderophores: fusigen, triacetylfusarinine C, and ferricrocin. Biosynthesis and uptake of iron from these siderophores, as well as from various heterologous siderophores, is repressed by iron and this regulation is mediated in part by the transcriptional repressor SREA. Recently we have characterized a putative siderophore-transporter-encoding gene ( mirA ). Here we present the characterization of two further SREA- and iron-regulated paralogues (mirB and mirC ), including the chromosomal localization and the complete exon/intron structure. Expression of mirA and mirB in a Saccharomyces cerevisiae strain, which lacks high affinity iron transport systems, showed that MIRA transports specifically the heterologous siderophore enterobactin and that MIRB transports exclusively the native siderophore triacetylfusarinine C. Construction and analysis of an A. nidulans mirA deletion mutant confirmed the substrate specificity of MIRA. Phylogenetic analysis of the available sequences suggests that the split of the species A. nidulans and S. cerevisiae predates the divergence of the paralogous Aspergillus siderophore transporters.

MeSH Terms
Amino Acid Sequence Aspergillus nidulans/classification,genetics,metabolism Bacterial Outer Membrane Proteins/genetics,metabolism Carrier Proteins/genetics,metabolism Cloning, Molecular Consensus Sequence DNA Primers Enterobactin/metabolism Exons Introns Iron/metabolism Membrane Transport Proteins/metabolism Molecular Sequence Data Phylogeny Plasmids Polymerase Chain Reaction Receptors, Cell Surface/genetics,metabolism Recombinant Proteins/metabolism Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins/metabolism Sequence Alignment Siderophores/metabolism
Chemicals
ARN2 protein, S cerevisiae Bacterial Outer Membrane Proteins Carrier Proteins DNA Primers Membrane Transport Proteins Receptors, Cell Surface Recombinant Proteins Saccharomyces cerevisiae Proteins Siderophores siderophore receptors Enterobactin Iron
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Haas Hubertus
Department of Molecular Biology, University of Innsbruck, Austria. hubertus.haas@uibk.ac.at
Schoeser Michelle
Lesuisse Emmanuel
Ernst Joachim F
Parson Walther
Abt Beate
Winkelmann Günther
Oberegger Harald
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/BJ20021685
Email
hubertus.haas@uibk.ac.at
Published
2003-04-15
Pages
505-13
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1223275
Subset
IM
Databases
GENBANK
AY131330, AY135152
External Links
PubMed source DOI: 10.1042/BJ20021685 PMC Full Text View journal details
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