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Mutations in thefacC gene ofAspergillus 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 thefacC 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 infacC mutants, while fatty acid-inducible activity was absent in anacuJ mutant. Acetate induction offacC expression was dependent on thefacB regulatory gene, and an expressed FacB fusion protein was demonstrated to bind to 5′facC sequences. Carbon catabolite repression offacC expression was affected by mutations in thecreA gene and a CreA fusion protein bound to 5′facC sequences. Mutations in theacuJ gene led to increased acetate induction offacC expression and also of anamdS-lacZ reporter gene, and it is proposed that this results from accumulation of acetate, as well as increased expression offacB . A model is presented in whichfacC encodes a cytosolic CAT enzyme, while a different CAT enzyme, which isacuJ dependent, is present in peroxisomes and mitochondria, and these activities are required for the movement of acetyl groups between intracellular compartments.

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