This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Davis, M. A.
Right arrow Articles by Hynes, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Davis, M. A.
Right arrow Articles by Hynes, M. J.
Agricola
Right arrow Articles by Davis, M. A.
Right arrow Articles by Hynes, M. J.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, July 2005, p. 3551-3555, Vol. 71, No. 7
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.7.3551-3555.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Amino Acid Catabolism by an areA-Regulated Gene Encoding an L-Amino Acid Oxidase with Broad Substrate Specificity in Aspergillus nidulans

Meryl A. Davis,* Marion C. Askin, and Michael J. Hynes

Department of Genetics, The University of Melbourne, Parkville 3010, Australia

Received 7 August 2004/ Accepted 13 January 2005

The filamentous fungus Aspergillus nidulans can use a wide range of compounds as nitrogen sources. The synthesis of the various catabolic enzymes needed to breakdown these nitrogen sources is regulated by the areA gene, which encodes a GATA transcription factor required to activate gene expression under nitrogen-limiting conditions. The areA102 mutation results in pleiotropic effects on nitrogen source utilization, including better growth on certain amino acids as nitrogen sources. Mutations in the sarA gene were previously isolated as suppressors of the strong growth of an areA102 strain on L-histidine as a sole nitrogen source. We cloned the sarA gene by complementation of a sarA mutant and showed that it encodes an L-amino acid oxidase enzyme with broad substrate specificity. Elevated expression of this enzyme activity in an areA102 background accounts for the strong growth of these strains on amino acids that are substrates for this enzyme. Loss of function sarA mutations, which abolish the L-amino acid oxidase activity, reverse the areA102 phenotype. Growth tests with areA102 and sarA mutants show that this enzyme is the primary route of catabolism for some amino acids, while other amino acids are metabolized through alternative pathways that yield either ammonium or glutamate for growth.


* Corresponding author. Mailing address: Department of Genetics, The University of Melbourne, Parkville 3010, Australia. Phone: 61-3-8344-5140. Fax: 61-3-8344-5139. E-mail: m.davis{at}unimelb.edu.au.


Applied and Environmental Microbiology, July 2005, p. 3551-3555, Vol. 71, No. 7
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.7.3551-3555.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Hynes, M. J., Murray, S. L., Duncan, A., Khew, G. S., Davis, M. A. (2006). Regulatory Genes Controlling Fatty Acid Catabolism and Peroxisomal Functions in the Filamentous Fungus Aspergillus nidulans. Eukaryot Cell 5: 794-805 [Abstract] [Full Text]