Nikaidou N, Kamio Y, Izaki K
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Biosci Biotechnol Biochem. 1993 Jun;57(6):957-60. doi: 10.1271/bbb.57.957.
Pectate lyase was purified approximately 29-fold to electrophoretic homogeneity from Pseudomonas marginalis N6301. A pectate lyase (PL; EC4.2.2.2) gene of the strain was cloned and expressed in Escherichia coli. The nucleotides of the PL gene (pel) were sequenced. An open reading frame that encodes a polypeptide (molecular weight: 40,812) composed of 380 amino acids including a 29 amino acid signal peptide was assigned. The structural gene of pel consisted of 1140 base pairs. The nucleotide sequence of the 5'-flanking region of pel showed a consensus sequence of the promoter region of the pectin lyase gene (pnl) in P. marginalis N6301, a Pribnow box, and a ribosome binding site as found in E. coli.
果胶酸裂解酶从边缘假单胞菌N6301中纯化至电泳纯,纯化倍数约为29倍。克隆了该菌株的果胶酸裂解酶(PL;EC4.2.2.2)基因,并在大肠杆菌中表达。对PL基因(pel)的核苷酸进行了测序。确定了一个开放阅读框,其编码由380个氨基酸组成的多肽(分子量:40812),其中包括一个29个氨基酸的信号肽。pel的结构基因由1140个碱基对组成。pel 5'侧翼区的核苷酸序列显示出边缘假单胞菌N6301中果胶裂解酶基因(pnl)启动子区的共有序列、一个Pribnow框以及大肠杆菌中发现的核糖体结合位点。