Abstract
It has been proposed that the bitopic membrane protein SecG undergoes topology inversion during translocation of (pre)proteins via SecYEG. Here we show that SecG covalently cross-linked to SecY cannot invert its topology while remaining fully functional in protein translocation. Our results strongly disfavor topology inversion of SecG during protein translocation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Biological Transport / physiology
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / physiology*
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Membrane Proteins / chemistry
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Membrane Proteins / physiology*
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Membrane Transport Proteins / chemistry
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Membrane Transport Proteins / physiology
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Protein Transport*
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SEC Translocation Channels
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Membrane Proteins
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Membrane Transport Proteins
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SEC Translocation Channels
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SecG protein, E coli