Morrice J, MacKenzie D A, Parr A J, Archer D B
Institute of Food Research, Norwich Research Park, Colney Lane, Norwich, Norfolk, NR4 7UA, UK.
Curr Genet. 1998 Dec;34(5):379-85. doi: 10.1007/s002940050410.
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.
已从构巢曲霉中分离出假定编码乙酰辅酶A羧化酶的基因accA。这个单拷贝基因有一个6864 bp的开放阅读框（ORF），并在5'端附近含有两个小内含子。通过逆转录聚合酶链反应（RT-PCR）在该基因的ATG起始密码子上游鉴定出一个短的开放阅读框。基于与其他生物的乙酰辅酶A羧化酶的序列同源性，已确定了假定的生物素、ATP、HCO3-和乙酰辅酶A结合位点。来自构巢曲霉的Northern数据和ACC酶活性测量表明，在以硝酸盐而非氨作为唯一氮源的培养基中，accA的表达更高。在构巢曲霉中删除accA未成功。构巢曲霉在添加了C16-18脂肪酸的ACC特异性抑制剂索拉芬A存在下无法生长，这表明ACC是一种必需酶。
