McCaman M T, Gabe J D
Mol Gen Genet. 1986 Jul;204(1):148-52. doi: 10.1007/BF00330202.
The pepN gene of Escherichia coli K-12 has been cloned onto a multi-copy plasmid and shown to encode a polypeptide which co-migrates with purified peptidase N. Transformed strains have been shown to contain up to a one hundred fold increase in the amount of peptidase N. We isolated the peptidase N protein and determined the sequence of its first 15 amino acids. By restriction mapping, we identified and subcloned the 5' region of the pepN gene and then determined its nucleotide sequence. Comparison of the actual amino acid sequence with that predicted from the extended open reading frame found in the DNA sequence indicated that peptidase N is not synthesized as a pre-protein precursor. The presumed region preceding the open reading frame contained nucleotide sequence having homology to the procaryotic promoter consensus sequences for the -35 and the -10 regions and the ribosome binding site.
大肠杆菌K-12的pepN基因已被克隆到多拷贝质粒上，并显示可编码一种与纯化的肽酶N共迁移的多肽。已证明转化菌株中肽酶N的含量增加了多达100倍。我们分离了肽酶N蛋白并确定了其前15个氨基酸的序列。通过限制性图谱分析，我们鉴定并亚克隆了pepN基因的5'区域，然后确定了其核苷酸序列。将实际氨基酸序列与从DNA序列中发现的延伸开放阅读框预测的序列进行比较，表明肽酶N不是以前体蛋白前体的形式合成的。开放阅读框之前的假定区域包含与原核生物启动子-35和-10区域以及核糖体结合位点的共有序列具有同源性的核苷酸序列。
