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. 2004 May 7;54(7):1003–1011. doi: 10.1016/0092-8674(88)90115-8

ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

Elliott Crooke 1, Brenda Guthrie 1, Stewart Lecker 1, Roland Lill 1, William Wickner 1
PMCID: PMC7133343  PMID: 2843289

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 post-ribosomal activity of SRP suggests a unifying theme in protein translocation mechanisms.

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