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J Biol Chem, Vol. 274, Issue 29, 20068-20070, July 16, 1999

COMMUNICATION
The Signal Recognition Particle-targeting Pathway Does Not Necessarily Deliver Proteins to the Sec-translocase in Escherichia coli

Susana Cristóbal, Pier Scotti^§, Joen Luirink^§, Gunnar von Heijne, and Jan-Willem L. de Gier

From the  Department of Biochemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden and the ^§ Department of Microbiology, BioCentrum Amsterdam, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands

ProW is an Escherichia coli inner membrane protein that consists of a 100-residue-long periplasmic N-terminal tail (N-tail) followed by seven closely spaced transmembrane segments. N-tail translocation presumably proceeds in a C-to-N-terminal direction and represents a poorly understood aspect of membrane protein biogenesis. Here, using an in vivo depletion approach, we show that N-tail translocation in a ProW derivative comprising the N-tail and the first transmembrane segment fused to the globular P2 domain of leader peptidase depends both on the bacterial signal recognition particle (SRP) and the Sec-translocase. Surprisingly, however, a deletion construct with only one transmembrane segment downstream of the N-tail can assemble properly even under severe depletion of SecE, a central component of the Sec-translocase, but not under SRP-depletion conditions. To our knowledge, this is the first demonstration that the SRP-targeting pathway does not necessarily deliver SRP-dependent inner membrane proteins to the Sec-translocase. The data further suggest that N-tail translocation can proceed in the absence of a functional Sec-translocase.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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