YidC mediates membrane protein insertion in bacteria

James C. Samuelson, Minyong Chen, Fenglei Jiang, Ines Möller, Martin Wiedmann, Andreas Kuhn, Gregory J. Phillips and Ross E. Dalbey ()
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James C. Samuelson: The Ohio State University
Minyong Chen: The Ohio State University
Fenglei Jiang: The Ohio State University
Ines Möller: Cellular Biochemistry and Biophysic Program, Memorial Sloan-Kettering Cancer Centre
Martin Wiedmann: Cellular Biochemistry and Biophysic Program, Memorial Sloan-Kettering Cancer Centre
Andreas Kuhn: University of Hohenheim, Institute for Microbiology and Molecular Biology
Gregory J. Phillips: Iowa State University
Ross E. Dalbey: The Ohio State University

Nature, 2000, vol. 406, issue 6796, 637-641

Abstract: Abstract The basic machinery for the translocation of proteins into or across membranes is remarkably conserved from Escherichia coli to humans. In eukaryotes, proteins are inserted into the endoplasmic reticulum using the signal recognition particle (SRP) and the SRP receptor, as well as the integral membrane Sec61 trimeric complex (composed of alpha, beta and gamma subunits)1. In bacteria, most proteins are inserted by a related pathway that includes the SRP homologue Ffh2,3,4,5, the SRP receptor FtsY6,7, and the SecYEG trimeric complex8, where Y and E are related to the Sec61 alpha and gamma subunits, respectively. Proteins in bacteria that exhibit no dependence on the Sec translocase were previously thought to insert into the membrane directly without the aid of a protein machinery9,10. Here we show that membrane insertion of two Sec-independent proteins requires YidC. YidC is essential for E. coli viability and homologues are present in mitochondria and chloroplasts. Depletion of YidC also interferes with insertion of Sec-dependent membrane proteins, but it has only a minor effect on the export of secretory proteins. These results provide evidence for an additional component of the translocation machinery that is specialized for the integration of membrane proteins.

Date: 2000
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DOI: 10.1038/35020586

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