Melchers K, Wiegert T, Buhmann A, Postius S, Schäfer K P, Schumann W
Institute of Genetics, University of Bayreuth, D-95440 Bayreuth, Germany.
Arch Microbiol. 1998 May;169(5):393-6. doi: 10.1007/s002030050588.
Cloning and sequencing of an approximately 6.0-kb chromosomal DNA fragment from Helicobacter felis revealed five complete open reading frames. The deduced amino acid sequence of one ORF exhibited sequence similarity to the FtsH protein, an ATP-dependent metalloprotease, from various bacterial species. The encoded protein consists of 638 amino acid residues with a molecular mass of 70.2 kDa. The hydropathy profile of the FtsH protein predicted two N-terminal transmembrane regions that were confirmed experimentally. Insertion of ftsH into a new versatile expression vector resulted in overexpression of FtsH protein in Escherichia coli. In addition, the E. coli ftsH gene could be replaced by the H. felis homologue to allow reduced growth and tenfold increased lysogenization by temperate phage lambda.
从猫螺杆菌中克隆并测序一段约6.0 kb的染色体DNA片段，发现了五个完整的开放阅读框。其中一个开放阅读框推导的氨基酸序列与来自多种细菌的FtsH蛋白（一种ATP依赖性金属蛋白酶）具有序列相似性。编码的蛋白质由638个氨基酸残基组成，分子量为70.2 kDa。FtsH蛋白的亲水性图谱预测有两个N端跨膜区域，这一点已通过实验得到证实。将ftsH插入一个新的通用表达载体，导致FtsH蛋白在大肠杆菌中过表达。此外，大肠杆菌的ftsH基因可被猫螺杆菌的同源物取代，从而使生长减缓，温和噬菌体λ的溶原化增加十倍。
