Tamaki T, Horinouchi S, Fukaya M, Okumura H, Kawamura Y, Beppu T
Department of Agricultural Chemistry, University of Tokyo.
J Biochem. 1989 Oct;106(4):541-4. doi: 10.1093/oxfordjournals.jbchem.a122889.
The nucleotide sequence of the membrane-bound aldehyde dehydrogenase (ALDH) gene from an industrial vinegar producer, Acetobacter polyoxogenes, was determined. Comparison of the sequence with the NH2-terminal amino acid sequence of the mature ALDH and determination of the actual translational initiation codon by means of in vitro manipulation of the upstream and proximal regions of the cloned gene showed that ALDH was primarily translated as a 773-amino-acid protein and that the 44-amino-acid sequence at the NH2-terminus, which probably serves as a signal peptide, was processed during maturation and localization in the membrane. When ALDH was expressed in a large quantity in Escherichia coli cells after the coding region had been placed downstream of the lac promoter, the ALDH protein, which still contained the signal peptide and had no ALDH activity, was localized in the membrane fraction.
测定了工业醋生产菌多氧醋酸杆菌膜结合醛脱氢酶（ALDH）基因的核苷酸序列。将该序列与成熟ALDH的氨基末端氨基酸序列进行比较，并通过对克隆基因上游和近端区域进行体外操作来确定实际的翻译起始密码子，结果表明，ALDH最初翻译为一种773个氨基酸的蛋白质，并且氨基末端的44个氨基酸序列可能作为信号肽，在成熟和膜定位过程中被加工。当编码区置于lac启动子下游后，在大肠杆菌细胞中大量表达ALDH时，仍含有信号肽且无ALDH活性的ALDH蛋白定位于膜部分。
