纯化的大肠杆菌触发因子或犬信号识别颗粒可使ProOmpA稳定以进行膜转运。
ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle.
作者信息
Crooke E, Guthrie B, Lecker S, Lill R, Wickner W
机构信息
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
出版信息
Cell. 1988 Sep 23;54(7):1003-11. doi: 10.1016/0092-8674(88)90115-8.
Abstract
We have isolated large amounts of E. coli outer-membrane protein A precursor (proOmpA). Purified proOmpA is active in membrane assembly, and this assembly is saturable with respect to the precursor protein. A proOmpA-Sepharose matrix allows affinity isolation of trigger factor, a soluble, 63,000 dalton monomeric protein that stabilizes proOmpA in assembly competent form. Comparison of trigger factor's amino-terminal sequence with those in a computer data bank and with those encoded by sec genes, as well as groEL and heat shock gene dnaK, suggests that trigger factor is encoded by a previously undescribed gene. Trigger factor and proOmpA form a 1:1 complex that can be isolated by gel filtration. Purified canine signal recognition particle (SRP) can also stabilize proOmpA for membrane insertion. This postribosomal activity of SRP suggests a unifying theme in protein translocation mechanisms.
摘要
我们已分离出大量大肠杆菌外膜蛋白A前体（proOmpA）。纯化后的proOmpA在膜组装中具有活性，并且这种组装相对于前体蛋白而言是可饱和的。一种proOmpA - 琼脂糖基质可用于亲和分离触发因子，这是一种可溶性的、63000道尔顿的单体蛋白，它能将proOmpA稳定为具有组装能力的形式。将触发因子的氨基末端序列与计算机数据库中的序列以及sec基因、groEL和热休克基因dnaK所编码的序列进行比较，结果表明触发因子是由一个先前未描述的基因编码的。触发因子与proOmpA形成1:1复合物，该复合物可通过凝胶过滤分离出来。纯化的犬信号识别颗粒（SRP）也能稳定proOmpA以便插入膜中。SRP的这种核糖体后活性提示了蛋白质转运机制中的一个统一主题。
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ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle.纯化的大肠杆菌触发因子或犬信号识别颗粒可使ProOmpA稳定以进行膜转运。
Cell. 1988 Sep 23;54(7):1003-11. doi: 10.1016/0092-8674(88)90115-8.
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