Pedersen S, Blumenthal R M, Reeh S, Russell L B, Lemaux P, Laursen R A, Nagarkatti S, Friesen J D
Proc Natl Acad Sci U S A. 1976 May;73(5):1698-701. doi: 10.1073/pnas.73.5.1698.
A previously isolated mutant of E. coli K12 HAK 88 [Kuwano, M., Endo, h & yamamoto, M. (1972) J. Bacteriol, 112, 1150-1156], contains a new protein that in two-dimensional gel electropherorgrams has the same molecular weight as normal elongation factor Tu, but whose isoelectric point is altered approximately 0.1 pH unit in the acidic direction. Peptide mapping, purification properties and the ratio of leucyl plus isoleucyl to methionyl plus cysteinyl residues of the normal elongation factor Tu protein and the new protein show a close similarity between the two. The mutation causing the altered electrophoretic mobility is located between argH and rif (79 min on the E. coli genetic map). These biochemical and genetic data indicate that strain HAK 88 has a mutationally altered tufB gene.
先前分离出的大肠杆菌K12 HAK 88突变体[久野,M.,远藤,H. & 山本,M.(1972年)《细菌学杂志》,112,1150 - 1156]含有一种新蛋白质,在二维凝胶电泳图谱中,其分子量与正常延伸因子Tu相同,但等电点在酸性方向上改变了约0.1个pH单位。正常延伸因子Tu蛋白和新蛋白的肽图、纯化特性以及亮氨酰加异亮氨酰与甲硫氨酰加半胱氨酰残基的比例显示二者非常相似。导致电泳迁移率改变的突变位于argH和rif之间(在大肠杆菌遗传图谱上为79分钟处)。这些生化和遗传数据表明,HAK 88菌株的tufB基因发生了突变。