Kanazawa H, Wu H C
J Bacteriol. 1979 Feb;137(2):818-23. doi: 10.1128/jb.137.2.818-823.1979.
Synthesis of cell envelope proteins was studied in ethylenediaminetetraacetic acid-lysozyme spheroplasts of Escherichia coli ML30. The rate of incorporation of [3H]arginine into proteins in spheroplasts was about 30% of that of intact cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins synthesized in spheroplasts revealed the preferential synthesis of five polypeptides, one of which has been identified as the free form of murein lipoprotein. Lipoprotein synthesized in spheroplasts was found to be of same molecular size as that of mature lipoprotein. No prolipoprotein was observed even with a short pulse-labeling with [3H]arginine. On the other hand, significant accumulation of newly synthesized lipoprotein in the cytoplasmic membrane fraction of spheroplasts was observed. These results suggest that the processing of prolipoprotein occurs in the cytoplasmic membrane fraction of the cell envelope.
在大肠杆菌ML30的乙二胺四乙酸 - 溶菌酶原生质体中研究了细胞包膜蛋白的合成。原生质体中[3H]精氨酸掺入蛋白质的速率约为完整细胞的30%。对原生质体中合成的蛋白质进行十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳,结果显示有五种多肽优先合成,其中一种已被鉴定为胞壁质脂蛋白的游离形式。发现原生质体中合成的脂蛋白与成熟脂蛋白具有相同的分子大小。即使对[3H]精氨酸进行短脉冲标记,也未观察到前脂蛋白。另一方面,在原生质体的细胞质膜部分观察到新合成的脂蛋白有明显积累。这些结果表明前脂蛋白的加工发生在细胞包膜的细胞质膜部分。