Cashman J S, Webster R E
J Bacteriol. 1977 Mar;129(3):1245-9. doi: 10.1128/jb.129.3.1245-1249.1977.
The major coat protein of the bacteriophage f1 is synthesized during infection of Escherichia coli and becomes tightly associated with the host membrane. This synthesis was studied in conjunction with the strain BB26-36, a mutant defective in phospholipid synthesis, to investigate basic questions concerning membrane protein and phospholipid synthesis. Coat protein synthesis is decreased in the absence of net phospholipid synthesis. The coat protein produced under these conditions is still found tightly associated with the membrane. Resumption of phospholipid synthesis leads to an increase in the synthesis and accumulation of the coat protein. Therefore, a correlation between coat protein and phospholipid synthesis seems to exist. However, the packaging of phage deoxyribonucleic acid into phage particles proceeds in the absence of phospholipid synthesis, and the number of phage particles produced appears to depend only on the amount of coat protein in the membrane.
噬菌体f1的主要外壳蛋白在感染大肠杆菌期间合成，并与宿主膜紧密结合。结合BB26 - 36菌株（一种磷脂合成缺陷型突变体）对这种合成进行了研究，以探讨有关膜蛋白和磷脂合成的基本问题。在没有净磷脂合成的情况下，外壳蛋白合成减少。在这些条件下产生的外壳蛋白仍与膜紧密结合。磷脂合成的恢复导致外壳蛋白合成和积累增加。因此，外壳蛋白和磷脂合成之间似乎存在相关性。然而，在没有磷脂合成的情况下，噬菌体脱氧核糖核酸包装到噬菌体颗粒中的过程仍在进行，产生的噬菌体颗粒数量似乎仅取决于膜中外壳蛋白的量。
