Yem D W, Wu H C
J Bacteriol. 1977 Sep;131(3):759-64. doi: 10.1128/jb.131.3.759-764.1977.
Mutants defective in the structure, biosynthesis, and assembly of murein lipoprotein have been isolated. One of these mutants has been shown to synthesize a structurally altered lipoprotein. The biochemical features of the mutant lipoprotein (lipid deficiency, dimer formation, and a reduced, bound form of lipoprotein) could be attributed to a single mutation (or closely linked mutations) located at 36.4 min of the Escherichia coli map. We propose that this mutant is altered in the structural gene for murein lipoprotein (mlpA). Biochemical studies carried out with a heterogenote, mlpA/F'mlpA+, revealed the biochemical codominance of the wild-type and mutant genes.
已分离出在胞壁质脂蛋白的结构、生物合成及组装方面存在缺陷的突变体。其中一个突变体已被证明能合成结构改变的脂蛋白。该突变脂蛋白的生化特性（脂质缺乏、二聚体形成以及脂蛋白结合形式减少）可归因于位于大肠杆菌染色体图谱36.4分钟处的单个突变（或紧密连锁的突变）。我们提出该突变体在胞壁质脂蛋白（mlpA）的结构基因上发生了改变。用异源基因mlpA/F'mlpA + 进行的生化研究揭示了野生型和突变基因的生化共显性。
