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Cellular and extracellular siderophores of Aspergillus nidulans and Penicillium chrysogenum

Charlang, Gisela and Ng, Bradford and Horowitz, Norman H. and Horowitz, Robert M. (1981) Cellular and extracellular siderophores of Aspergillus nidulans and Penicillium chrysogenum. Molecular and Cellular Biology, 1 (2). pp. 94-100. ISSN 0270-7306. http://resolver.caltech.edu/CaltechAUTHORS:CHAmcb81

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Abstract

Aspergillus nidulans and Penicillium chrysogenum produce specific cellular siderophores in addition to the well-known siderophores of the culture medium. Since this was found previously in Neurospora crassa, it is probably generally true for filamentous ascomycetes. The cellular siderophore of A. nidulans is ferricrocin; that of P. chrysogenum is ferrichrome. A. nidulans also contains triacetylfusigen, a siderophore without apparent biological activity. Conidia of both species lose siderophores at high salt concentrations and become siderophore dependent. This has also been found in N. crassa, where lowering of the water activity has been shown to be the causal factor. We used an assay procedure based on this dependency to reexamine the extracellular siderophores of these species. During rapid mycelial growth, both A. nidulans and P. chrysogenum produced two highly active, unidentified siderophores which were later replaced by a less active or inactive product--coprogen in the case of P. chrysogenum and triacetylfusigen in the case of A. nidulans. N. crassa secreted coprogen only. Fungal siderophore metabolism is varied and complex.


Item Type:Article
Additional Information:Copyright © 1981 by the American Society for Microbiology. This research was supported by Public Health Service grant AI15739 from the National Institute of Allergy and Infectious Diseases and by Biomedical Research Support Grant SO7 RR07003 from the Division of Research Resources, National Institutes of Health. We are greatly indebted to Thomas Emery for a sample of N,N',N"-triacetylfusarinine-C and to W. Keiler-Schierlein for samples of ferrichrome and ferricrocin. We thank J. Roger Shelton for performing the amino acid analyses.
Record Number:CaltechAUTHORS:CHAmcb81
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:CHAmcb81
Alternative URL:http://mcb.asm.org/cgi/content/abstract/1/2/94
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:2282
Collection:CaltechAUTHORS
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Deposited On:21 Mar 2006
Last Modified:26 Dec 2012 08:48

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