Abstract
Previous work showed that SecA alone can promote protein translocation and ion-channel activity in liposomes, and that SecYEG increases efficiency as well as signal peptide specificity. We now report that SecDF·YajC further increases translocation and ion-channel activity. These activities of reconstituted SecA-SecYEG-SecDF·YajC-liposome are almost the same as those of native membranes, indicating the transformation of reconstituted functional high-affinity protein-conducting channels from the low-affinity SecA-channels.
Published by Elsevier Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / metabolism*
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism*
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Ion Channels / chemistry
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Ion Channels / metabolism*
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Liposomes / chemistry
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Liposomes / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Membrane Transport Proteins / chemistry
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Membrane Transport Proteins / metabolism*
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Protein Transport
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SEC Translocation Channels
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SecA Proteins
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Xenopus laevis
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Ion Channels
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Liposomes
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Membrane Proteins
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Membrane Transport Proteins
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SEC Translocation Channels
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SecD protein, E coli
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SecF protein, E coli
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Adenosine Triphosphatases
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SecA Proteins