大肠杆菌中膜衍生寡糖生物合成的渗透调节
Osmotic regulation of biosynthesis of membrane-derived oligosaccharides in Escherichia coli.
作者信息
Kennedy E P, Rumley M K
机构信息
Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115.
出版信息
J Bacteriol. 1988 Jun;170(6):2457-61. doi: 10.1128/jb.170.6.2457-2461.1988.
The osmotic regulation of the biosynthesis of membrane-derived oligosaccharides (MDO) in strains UB1005 and DC2 of Escherichia coli K-12 was examined; this regulation was previously reported by Clark (J. Bacteriol. 161:1049-1053, 1985) to be different from that observed by Kennedy for other strains of E. coli (Proc. Natl. Acad. Sci. USA 79:1092-1095, 1982). Osmotic regulation of the synthesis of MDO in UB1005 and DC2 is in fact indistinguishable from that previously reported for other strains of E. coli, with maximum production of MDO occurring in the medium of lowest osmolarity. The report of Clark to the contrary was apparently based on the inadequate methods for the measurement of MDO employed in that study. MDO are localized in the periplasm of wild-type E. coli cells. However, strain DC2, selected for hypersensitivity to a range of antibiotics, released most of its MDO into the medium, apparently as a result of greater outer membrane permeability.
对大肠杆菌K - 12菌株UB1005和DC2中膜衍生寡糖（MDO）生物合成的渗透调节进行了研究；克拉克之前报道过（《细菌学杂志》161:1049 - 1053，1985年），这种调节与肯尼迪在其他大肠杆菌菌株中观察到的不同（《美国国家科学院院刊》79:1092 - 1095，1982年）。实际上，UB1005和DC2中MDO合成的渗透调节与之前报道的其他大肠杆菌菌株的调节并无区别，MDO在最低渗透压的培养基中产量最高。克拉克的相反报告显然是基于该研究中用于测量MDO的方法不充分。MDO定位于野生型大肠杆菌细胞的周质中。然而，因对一系列抗生素超敏而选择的DC2菌株，显然由于外膜通透性更高，将其大部分MDO释放到了培养基中。
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