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A more recent version of this article appeared on April 14, 2006
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M511357200v1
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Papers In Press, published online ahead of print February 15, 2006
J. Biol. Chem, 10.1074/jbc.M511357200
Submitted on October 19, 2005
Revised on January 26, 2006
Accepted on February 15, 2006

Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CYOA

Edwin van Bloois, Gert-Jan Haan, Jan-Willem de Gier, Bauke Oudega, and Joen Luirink

Department of Microbiology, Institute of Molecular Biological Sciences, Amsterdam 1081 HV

Corresponding Author: luirink{at}bio.vu.nl

Inner membrane proteins (IMPs) of Escherichia coli use different pathways for membrane targeting and integration. YidC plays an essential but poorly defined role in the integration and folding of IMPs both in conjunction with the Sec-translocon and as a Sec-independent insertase. Depletion of YidC only marginally affects the insertion of Sec-dependent IMPs, whereas it blocks the insertion of a subset of Sec-independent IMPs. Substrates of this latter “YidC-only” pathway include the relatively small IMPs M13 procoat, Pf3 coat protein and subunit c of the F1F0 ATPase. Recently, it has been shown that the steady state level of the larger and more complex CyoA subunit of the cytochrome o oxidase is also severely affected upon depletion of YidC. In the present study, we have analyzed the biogenesis of the integral lipoprotein CyoA. Collectively, our data suggest that the first transmembrane segment (TM) of CyoA rather than the signal sequence recruits the SRP for membrane targeting. Membrane integration and assembly appears to occur in two distinct sequential steps. YidC is sufficient to catalyze insertion of the N-terminal domain consisting of the signal sequence, TM1 and the small periplasmic domain in between. Translocation of the large C-terminal periplasmic domain requires the Sec-translocon and SecA suggesting that for this particular IMP, the Sec-translocon might operate downstream of YidC.


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