Abstract
Previous studies have proposed that the N-terminal A domain (approximately 200 amino acid residues) of the Escherichia coli signal recognition particle (SRP) receptor, FtsY, is required for membrane targeting. In contrast to this suggestion, we show that A domain-truncated versions of FtsY, harboring only domains N and G, are functional. Therefore, we propose that N and G domains constitute the core SRP receptor.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / analysis
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Blotting, Western
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Cell Membrane / metabolism
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Escherichia coli / metabolism*
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Escherichia coli Proteins / analysis
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Genetic Complementation Test
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Protein Structure, Tertiary
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Receptors, Cytoplasmic and Nuclear / analysis
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Receptors, Cytoplasmic and Nuclear / genetics
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Signal Recognition Particle / metabolism
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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FtsY protein, Bacteria
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Receptors, Cytoplasmic and Nuclear
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Signal Recognition Particle