In vitro trimerization of OmpF porin secreted by spheroplasts of Escherichia coli.
In vitro trimerization of OmpF porin secreted by spheroplasts of Escherichia coli.
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大肠杆菌原生质球分泌的 OmpF 孔蛋白的体外三聚化。
DOI：
10.1073/pnas.87.2.743
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发表时间：
1990
影响因子：
11.1
通讯作者：
Nikaido,H
中科院分区：
文献类型：
--
作者：
Sen,K;Nikaido,H
目前尚不清楚细菌外膜蛋白在通过细胞质膜分泌后如何到达正确的目的地。我们在这里表明，孔蛋白OmpF是由大肠杆菌的球体分泌到培养上清液中的水溶性单体蛋白。此外，在0.03%的Triton X-100存在下，这种单体孔蛋白被细胞被膜制剂或纯化的脂多糖吸收，并被正确地转化为成熟的三聚体构象。这些结果似乎复制了这种蛋白质的部分生理输出和靶向步骤。
It is not yet clear how bacterial outer membrane proteins reach their correct destination after they are secreted across the cytoplasmic membrane. We show here that porin OmpF is secreted into the medium as a water-soluble monomeric protein by spheroplasts of Escherichia coli. Furthermore, this monomeric porin is taken up by cell envelope preparations or purified lipopolysaccharides in the presence of 0.03% Triton X-100 and is converted correctly into the mature trimeric conformation. These results appear to reproduce a part of the physiological export and targeting steps of this protein.