Abstract
Microcin C (McC), a natural antibacterial compound consisting of a heptapeptide attached to a modified adenosine, is actively taken up by the YejABEF transporter, after which it is processed by cellular aminopeptidases, releasing the nonhydrolyzable aminoacyl adenylate, an inhibitor of aspartyl-tRNA synthetase. McC analogues with variable length of the peptide moiety were synthesized and evaluated in order to characterize the substrate preferences of the YejABEF transporter. It was shown that a minimal peptide chain length of 6 amino acids and the presence of an N-terminal formyl-methionyl-arginyl sequence are required for transport.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Binding Cassette Transporters / genetics
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ATP-Binding Cassette Transporters / metabolism*
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / metabolism*
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Bacteriocins / chemistry
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Bacteriocins / metabolism*
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Biological Transport
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Escherichia coli / chemistry
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Molecular Structure
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Peptides / chemistry*
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Peptides / genetics
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Peptides / metabolism
Substances
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ATP-Binding Cassette Transporters
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Anti-Bacterial Agents
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Bacteriocins
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Escherichia coli Proteins
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Peptides
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microcin