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Journal of Bacteriology, October 2003, p. 5697-5705, Vol. 185, No. 19
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.19.5697-5705.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli

Christina Wilson Bowers, Fion Lau, and Thomas J. Silhavy*

Department of Molecular Biology, Princeton University, Princeton, New Jersey

Received 1 May 2003/ Accepted 26 June 2003

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.

* Corresponding author. Mailing address: Department of Molecular Biology, Princeton University, Princeton, NJ 08544. Phone: (609) 258-5899. Fax: (609) 258-2957. E-mail: tsilhavy{at}molbio.princeton.edu.

Journal of Bacteriology, October 2003, p. 5697-5705, Vol. 185, No. 19
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.19.5697-5705.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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