Abstract
The putative gene encoding acetyl-CoA carboxylase, accA, has been isolated from Aspergillus nidulans. This single-copy gene has an open reading frame (ORF) of 6864 bp and contains two small introns near the 5′-end. A short ORF upstream of the ATG start codon has been identified in this gene by RT-PCR. Based on sequence homology to acetyl-CoA carboxylases from other organisms, putative biotin-, ATP-, HCO3 –- and acetyl-CoA- binding sites have been assigned. Northern data and ACC enzyme-activity measurements from A. nidulans suggested that expression of accA was higher in media containing nitrate than ammonia as a sole nitrogen source. Deletion of accA in A. nidulans was unsuccessful. The failure of A. nidulans to grow in the presence of the ACC-specific inhibitor, soraphen A, supplemented with C16–18 fatty acids suggested that ACC is an essential enzyme.
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Received: 29 January / 26 September 1998
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Morrice, J., MacKenzie, D., Parr, A. et al. Isolation and characterisation of the acetyl-CoA carboxylase gene from Aspergillus nidulans. Curr Genet 34, 379–385 (1998). https://doi.org/10.1007/s002940050410
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DOI: https://doi.org/10.1007/s002940050410