P. Heymann et al., Identification and substrate specificity of a ferrichrome-type siderophoretransporter (Arn1p) in Saccharomyces cerevisiae, FEMS MICROB, 186(2), 2000, pp. 221-227
Genes encoding transporters for heterologous siderophores have been identif
ied in Saccharomyces cerevisiae, of which SIT1; TAF1, and ENB1 encode the t
ransporters for ferrioxamines, ferric triacetylfursarinine C and ferric ent
erobactin, respectively. In the present communication we have shown that a
further gene encoding a member of the major facilitator superfamily, ARN1 (
YHL040c), is involved in the transport of a specific class of ferrichromes,
possessing anhydromevalonyl residues linked to N-delta-ornithine (ARN). Fe
rrirubin and ferrirhodin, which both are produced by filamentous fungi, are
the most common representatives of this class of ferrichromes. A strain po
ssessing a disruption in the ARN1 gene was unable to transport ferrirubin,
ferrirhodin and also ferrichrome A, indicating that the encoded transporter
recognizes anhydromevalonyl and the structurally-related methylglutaconyl
side-chains surrounding the iron center. Ferrichromes possessing short-chai
n ornithine-N-delta-acetyl residues such as ferrichrome, ferricrocin and fe
rrichrysin, were excluded by the Arn1 transporter. Substitution of the iron
-surrounding N-acyl chains of ferrichromes by propionyl residues had no eff
ect, whereas substitution by butyryl residues led to recognition by the Aml
transporter. This would indicate that a chain length of four C-atoms is su
fficient to allow binding. Using different asperchromes (B1, Di) we also fo
und that a minimal number of two anhydromevalonyl residues is sufficient fo
r recognition by Arn Ip. Contrary to the iron-surrounding N-acyl residues,
the peptide backbone of ferrichromes was not an important determinant for t
he Arn1 transporter. (C) 2000 Federation of European Microbiological Societ
ies. Published by Elsevier Science B.V. All rights reserved.