@article{89831,
  keywords = {Hydrophobic and Hydrophilic Interactions, signal transduction, Escherichia coli, Recombinant Fusion Proteins, Protein Biosynthesis, Escherichia coli Proteins, Protein Sorting Signals, Bacterial Outer Membrane Proteins, Receptors, Virus, Lac Operon, Porins, Signal Recognition Particle},
  author = {Christina Wilson Bowers and Fion Lau and Thomas Silhavy},
  title = {Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli},
  abstract = {<p>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.</p>
},
  year = {2003},
  journal = {J Bacteriol},
  volume = {185},
  pages = {5697-705},
  month = {10/2003},
  issn = {0021-9193},
  doi = {10.1128/JB.185.19.5697-5705.2003},
  language = {eng},
}