PMID:2843289
| Citation |
Crooke, E, Guthrie, B, Lecker, S, Lill, R and Wickner, W (1988) ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle. Cell 54:1003-11 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Isomerases/isolation & purification; Amino Acid Isomerases/physiology; Animals; Bacterial Outer Membrane Proteins/isolation & purification; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/isolation & purification; Bacterial Proteins/physiology; Biological Transport; Carrier Proteins/isolation & purification; Carrier Proteins/physiology; Chromatography, Liquid; Dogs; Escherichia coli/metabolism; Escherichia coli Proteins; Membranes/metabolism; Microsomes/metabolism; Pancreas/metabolism; Peptidylprolyl Isomerase; Protein Binding; Protein Precursors/isolation & purification; Protein Precursors/metabolism; Ribonucleoproteins/pharmacology; Signal Recognition Particle |
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