Tomoyasu T, Yuki T, Morimura S, Mori H, Yamanaka K, Niki H, Hiraga S, Ogura T
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan.
J Bacteriol. 1993 Mar;175(5):1344-51. doi: 10.1128/jb.175.5.1344-1351.1993.
The ftsH gene is essential for cell viability in Escherichia coli. We cloned and sequenced the wild-type ftsH gene and the temperature-sensitive ftsH1(Ts) gene. It was suggested that FtsH protein was an integral membrane protein of 70.7 kDa (644 amino acid residues) with a putative ATP-binding domain. The ftsH1(Ts) gene was found to have two base substitutions within the coding sequence corresponding to the amino acid substitutions Glu-463 by Lys and Pro-587 by Ala. Homology search revealed that an approximately 200-amino-acid domain, including the putative ATP-binding sequence, is highly homologous (35 to 48% identical) to the domain found in members of a novel, eukaryotic family of putative ATPases, e.g., Sec18p, Pas1p, CDC48p, and TBP-1, which function in protein transport pathways, peroxisome assembly, cell division cycle, and gene expression, respectively. Possible implications of these observations are discussed.
ftsH基因对大肠杆菌的细胞生存能力至关重要。我们克隆并测序了野生型ftsH基因和温度敏感型ftsH1（Ts）基因。研究表明，FtsH蛋白是一种70.7 kDa（644个氨基酸残基）的整合膜蛋白，具有一个假定的ATP结合结构域。发现ftsH1（Ts）基因在编码序列内有两个碱基替换，分别对应氨基酸替换：Glu-463被Lys替换以及Pro-587被Ala替换。同源性搜索显示，一个约200个氨基酸的结构域，包括假定的ATP结合序列，与一个新的真核假定ATP酶家族成员中发现的结构域高度同源（同一性为35%至48%），例如Sec18p、Pas1p、CDC48p和TBP-1，它们分别在蛋白质转运途径、过氧化物酶体组装、细胞分裂周期和基因表达中发挥作用。本文讨论了这些观察结果的可能意义。
