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| The EMBO Journal
(2000) 19, 852–861, doi:10.1093/emboj/19.5.852 |
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| SecYEG assembles into a tetramer to form the active protein translocation channel |
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| Erik H. Manting1, Chris van der Does1, Hervé Remigy2, Andreas Engel2 and Arnold J. M. Driessen1 |
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1 Department of Microbiology and Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands 2 The Maurice E.Müller-Institute for Microscopy, Biozentrum of the University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland To whom correspondence should be addressed Arnold J. M. Driessen, A.J.M.Driessen@biol.rug.nl Received 11 June 1999; Revised 5 January 2000; Accepted 12 January 2000. |
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| Abstract |
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Translocase mediates preprotein translocation across the Escherichia coli inner membrane. It consists of the SecYEG integral membrane protein complex and the peripheral ATPase SecA. Here we show by functional assays, negative-stain electron microscopy and mass measurements with the scanning transmission microscope that SecA recruits SecYEG complexes to form the active translocation channel. The active assembly of SecYEG has a side length of 10.5 nm and exhibits an  5 nm central cavity. The mass and structure of this SecYEG as well as the subunit stoichiometry of SecA and SecY in a soluble translocase–precursor complex reveal that translocase consists of the SecA homodimer and four SecYEG complexes. |
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| Keywords: preprotein translocation, SecA, SecY, translocase |
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