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Characterization of peptide chain length and constituency requirements for YejABEF-mediated uptake of microcin C analogues.


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.

SUBMITTER: Vondenhoff GH 

PROVIDER: S-EPMC3133342 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Characterization of peptide chain length and constituency requirements for YejABEF-mediated uptake of microcin C analogues.

Vondenhoff Gaston H M GH   Blanchaert Bart B   Geboers Sophie S   Kazakov Teymur T   Datsenko Kirill A KA   Wanner Barry L BL   Rozenski Jef J   Severinov Konstantin K   Van Aerschot Arthur A  

Journal of bacteriology 20110520 14


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  ...[more]

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