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 Stemple, C. J.
Right arrow Articles by Hynes, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stemple, C. J.
Right arrow Articles by Hynes, M. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 1998, p. 6242-6251, Vol. 180, No. 23
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The facC Gene of Aspergillus nidulans Encodes an Acetate-Inducible Carnitine Acetyltransferase

Christopher J. Stemple, Meryl A. Davis, and Michael J. Hynes*

Department of Genetics, The University of Melbourne, Parkville, Victoria 3052, Australia

Received 11 May 1998/Accepted 1 October 1998

Mutations in the facC gene of Aspergillus nidulans result in an inability to use acetate as a sole carbon source. This gene has been cloned by complementation. The proposed translation product of the facC gene has significant similarity to carnitine acetyltransferases (CAT) from other organisms. Total CAT activity was found to be inducible by acetate and fatty acids and repressed by glucose. Acetate-inducible activity was found to be absent in facC mutants, while fatty acid-inducible activity was absent in an acuJ mutant. Acetate induction of facC expression was dependent on the facB regulatory gene, and an expressed FacB fusion protein was demonstrated to bind to 5' facC sequences. Carbon catabolite repression of facC expression was affected by mutations in the creA gene and a CreA fusion protein bound to 5' facC sequences. Mutations in the acuJ gene led to increased acetate induction of facC expression and also of an amdS-lacZ reporter gene, and it is proposed that this results from accumulation of acetate, as well as increased expression of facB. A model is presented in which facC encodes a cytosolic CAT enzyme, while a different CAT enzyme, which is acuJ dependent, is present in peroxisomes and mitochondria, and these activities are required for the movement of acetyl groups between intracellular compartments.

* Corresponding author. Mailing address: Department of Genetics, University of Melbourne, Parkville, Victoria 3052, Australia. Phone: (61 3) 9344 6246. Fax: (61 3) 9344 5139. E-mail: hynes.lab{at}genetics.unimelb.edu.au.

Journal of Bacteriology, December 1998, p. 6242-6251, Vol. 180, No. 23
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hynes, M. J., Szewczyk, E., Murray, S. L., Suzuki, Y., Davis, M. A., Sealy-Lewis, H. M. (2007). Transcriptional Control of Gluconeogenesis in Aspergillus nidulans. Genetics 176: 139-150 [Abstract] [Full Text]  
  • 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]  
  • Hynes, M. J., Draht, O. W., Davis, M. A. (2002). Regulation of the acuF Gene, Encoding Phosphoenolpyruvate Carboxykinase in the Filamentous Fungus Aspergillus nidulans. J. Bacteriol. 184: 183-190 [Abstract] [Full Text]  
  • Szewczyk, E., Andrianopoulos, A., Davis, M. A., Hynes, M. J. (2001). A Single Gene Produces Mitochondrial, Cytoplasmic, and Peroxisomal NADP-dependent Isocitrate Dehydrogenase in Aspergillus nidulans. J. Biol. Chem. 276: 37722-37729 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»