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YidC mediates membrane protein insertion in bacteria

Nature volume 406, pages 637–641 (2000)Cite this article

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.

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Figure 1: Genotype and phenotype of YidC-depletion strain JS7131.
Figure 2: Effect of YidC depletion on the translocation of pre-proteins.
Figure 3: YidC is required for efficient membrane insertion of Sec-independent and Sec-dependent proteins as determined by a protease accessibility assay.
Figure 4: Crosslinking of T7Lep to YidC.

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Acknowledgements

We thank P. G. Schultz for the E. coli suppressor tRNAAsn gene, S. R. Kushner for knockout vector pMAK705, J.-W. de Gier for the ProW construct, J. Brunner for the photocrosslinking reagent (Tmd)Phe-pdCpA, and Matthias Muller for advice with the amber suppression studies. This work was supported by an NSF grant (to R.E.D) and by a DFG grant (to A.K.).

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Authors and Affiliations

  1. Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus , 43210, Ohio, USA

    James C. Samuelson, Minyong Chen, Fenglei Jiang & Ross E. Dalbey

  2. Cellular Biochemistry and Biophysic Program, Memorial Sloan-Kettering Cancer Centre, 1275 York Avenue , New York, New York, 10021, USA

    Ines Möller & Martin Wiedmann

  3. University of Hohenheim, Institute for Microbiology and Molecular Biology, Garbenstrasse 30, Stuttgart, D-70599, Germany

    Andreas Kuhn

  4. Department of Microbiology, Iowa State University, 207 Science I, Osborn Drive, Ames, 50011, Iowa, USA

    Gregory J. Phillips

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Correspondence to Ross E. Dalbey.

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Samuelson, J., Chen, M., Jiang, F. et al. YidC mediates membrane protein insertion in bacteria. Nature 406, 637–641 (2000). https://doi.org/10.1038/35020586

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