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Journal of Bacteriology, December 1998, p. 6242-6251, Vol. 180, No. 23
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.
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
*
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.
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