Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase.
Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase.
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DOI：
10.1016/s0021-9258(18)33964-4
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发表时间：
1982-09
期刊：
影响因子：
--
通讯作者：
M. Tokunaga;J. Loranger;P. Wolfe;H. C. Wu
中科院分区：
文献类型：
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作者：
M. Tokunaga;J. Loranger;P. Wolfe;H. C. Wu
我们先前已经报道了在大肠杆菌细胞包膜中的信号肽酶活性，其加工用甘油酯修饰的前脂蛋白（Tokunaga，M.，Tokunaga，H.，和Wu，H. C.等人（1982）Proc. Acad. Sci.联合S. A. 79，2255-2259）。为了确定前脂蛋白的加工酶是否不同于由Zwizinski和Wickner纯化的M13前外壳蛋白的信号肽酶（Zwizinski，C.，和Wickner，W.（1980）J.Biol.Chem.255，7973-7977），我们已经使用抗纯化的前外壳蛋白信号肽酶的抗体来研究前脂蛋白和M13前外壳蛋白的体外加工。修饰的前脂蛋白的信号肽酶在用抗纯化的前外壳蛋白信号肽酶的抗体处理的溶解的膜制剂中保持完全活性，而对前外壳蛋白的活性被免疫吸附完全消除。此外，未修饰的和甘油酯修饰的前脂蛋白不被Wickner提供的高度纯化的信号肽酶制剂裂解。这些数据清楚地表明，前脂蛋白信号肽酶不同于M13前外壳蛋白信号肽酶。
We have previously reported a signal peptidase activity in Escherichia coli cell envelope which processes prolipoprotein modified with glyceride (Tokunaga, M., Tokunaga, H., and Wu, H. C. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 2255-2259). To ascertain whether the processing enzyme for prolipoprotein is distinct from the signal peptidase for M13 procoat protein purified by Zwizinski and Wickner (Zwizinski, C., and Wickner, W. (1980) J. Biol. Chem. 255, 7973-7977), we have used antibody against purified procoat protein signal peptidase to study the processings of prolipoprotein and M13 procoat protein in vitro. the signal peptidase for modified prolipoprotein remained fully active in solubilized membrane preparations which had been treated with antibody against purified procoat protein signal peptidase whereas the activity towards procoat protein was completely abolished by immunoadsorption. Furthermore, both unmodified and glyceride-modified prolipoprotein were not cleaved by the highly purified signal peptidase preparation provided by Wickner. These data clearly indicate that prolipoprotein signal peptidase is distinct from the M13 procoat protein signal peptidase.