Characterization of peptide chain length and constituency requirements for YejABEF-mediated uptake of microcin C analogues.
J Bacteriol
; 193(14): 3618-23, 2011 Jul.
Article
em En
| MEDLINE
| ID: mdl-21602342
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Bacteriocinas
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Transportadores de Cassetes de Ligação de ATP
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Proteínas de Escherichia coli
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Escherichia coli
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Antibacterianos
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article