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

Gaston H.M. Vondenhoff, Bart Blanchaert, Sophie Geboers, Teymur Kazakov, Kirill A. Datsenko, Barry L. Wanner, Jef Rozenski, Konstantin Severinov, Arthur Van Aerschot

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)3618-3623
Number of pages6
JournalJournal of bacteriology
Volume193
Issue number14
DOIs
StatePublished - Jul 2011

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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