Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli
| Autor: | Thomas J. Silhavy, Fion K. Lau, Christina Wilson Bowers |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Signal peptide
Recombinant Fusion Proteins Porins Protein Sorting Signals medicine.disease_cause environment and public health Microbiology Microbial Cell Biology Escherichia coli medicine Secretion Molecular Biology Signal recognition particle biology Escherichia coli Proteins Periplasmic space Fusion protein Cell biology Lac Operon Biochemistry Protein Biosynthesis Chaperone (protein) biology.protein Receptors Virus Signal transduction Hydrophobic and Hydrophilic Interactions Signal Recognition Particle Bacterial Outer Membrane Proteins Signal Transduction |
| Zdroj: | Journal of Bacteriology. 185:5697-5705 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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