Robbins A R, Rotman B
Proc Natl Acad Sci U S A. 1972 Aug;69(8):2125-9. doi: 10.1073/pnas.69.8.2125.
The activity of the methylgalactoside transport system of E. coli is impaired upon treatment with 3-decynoyl-N-acetylcysteamine, an inhibitor of unsaturated fatty-acid synthesis. Treated cells are unable to be induced for permease activity, while transport sites synthesized before treatment show a regular loss of activity. The inhibition of methylgalactoside transport occurs at a step after translation of the galactose-binding protein, a component of the permease, and appears to be highly specific, since drug-treated cells show normal viability, protein synthesis, and membrane integrity when transport activity is greatly reduced. A second transport system, the galactoside permease, shows significantly less sensitivity to the inhibitor. That the activity of this permease is maintained in the presence of this inhibitor suggests that the inhibitor does not impair energy coupling.
用3-癸炔酰-N-乙酰半胱胺（一种不饱和脂肪酸合成抑制剂）处理后，大肠杆菌甲基半乳糖苷转运系统的活性受损。经处理的细胞无法被诱导产生通透酶活性，而在处理前合成的转运位点则呈现出活性的规律性丧失。甲基半乳糖苷转运的抑制发生在通透酶组分半乳糖结合蛋白翻译后的一个步骤，并且似乎具有高度特异性，因为当转运活性大幅降低时，经药物处理的细胞仍表现出正常的活力、蛋白质合成和膜完整性。第二个转运系统，即半乳糖苷通透酶，对该抑制剂的敏感性明显较低。在该抑制剂存在的情况下这种通透酶的活性得以维持，这表明该抑制剂不会损害能量偶联。
