PMID:13129940
| Citation |
Bowers, CW, Lau, F and Silhavy, TJ (2003) Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli. J. Bacteriol. 185:5697-705 |
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| Abstract |
LamB-LacZ fusion proteins have classically been used in studies of the general secretion pathway of Escherichia coli. Here we describe how increasing signal sequence hydrophobicity routes LamB-LacZ Hyb42-1 to the signal recognition particle (SRP) pathway. Secretion of this hydrophobic fusion variant (H*LamB-LacZ) was reduced in the absence of fully functional Ffh and Ffs, and the translocator jamming caused by Hyb42-1 was prevented by efficient delivery of the fusion to the periplasm. Finally, we found that in the absence of the ribosome-associated chaperone, trigger factor (Tig), LamB-LacZ localized to the periplasm in a SecA-dependent, SRP-independent fashion. Collectively, our results provide compelling in vivo evidence that there is an SRP-dependent cotranslational targeting mechanism in E. coli and argue against a role for trigger factor in pathway discrimination. |
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| Keywords |
Bacterial Outer Membrane Proteins; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrophobic and Hydrophilic Interactions; Lac Operon; Porins; Protein Biosynthesis; Protein Sorting Signals; Receptors, Virus/genetics; Receptors, Virus/metabolism; Recombinant Fusion Proteins/metabolism; Signal Recognition Particle/metabolism; Signal Transduction |
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