The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex

The SecYEG complex is a major component of the protein translocation apparatus in the cytoplasmic membrane of bacteria. We have purified a translocationally active complex of the two subunits, SecY and SecE, from Bacillus subtilis. As demonstrated by electron microscopy, SecY/E forms ring structures...

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Bibliographic Details
Published in:Journal of molecular biology 1999-01, Vol.285 (4), p.1789-1800
Main Authors: Meyer, T H, Ménétret, J F, Breitling, R, Miller, K R, Akey, C W, Rapoport, T A
Format: Article
Language:English
Subjects:
Bacillus subtilis - chemistry
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bacterial Proteins - ultrastructure
Biological Transport, Active
Detergents
Escherichia coli - genetics
Escherichia coli Proteins
Gene Expression
Macromolecular Substances
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Microscopy, Electron
Protein Conformation
Proteolipids
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
SEC Translocation Channels
Solutions
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Summary:The SecYEG complex is a major component of the protein translocation apparatus in the cytoplasmic membrane of bacteria. We have purified a translocationally active complex of the two subunits, SecY and SecE, from Bacillus subtilis. As demonstrated by electron microscopy, SecY/E forms ring structures in detergent solution and in intact lipid bilayers, often with a quasi-pentagonal appearance in projection. The particles represent oligomeric assemblies of the SecY/E complex and are similar to those formed by the eukaryotic Sec61p complex. We propose that these SecY/E rings represent protein-conducting channels and that the two essential membrane components SecY and SecE are sufficient for their formation.
ISSN:0022-2836
DOI:10.1006/jmbi.1998.2413