TY - JOUR
T1 - Characterization of peptide chain length and constituency requirements for YejABEF-mediated uptake of microcin C analogues
AU - Vondenhoff, Gaston H.M.
AU - Blanchaert, Bart
AU - Geboers, Sophie
AU - Kazakov, Teymur
AU - Datsenko, Kirill A.
AU - Wanner, Barry L.
AU - Rozenski, Jef
AU - Severinov, Konstantin
AU - Van Aerschot, Arthur
PY - 2011/7
Y1 - 2011/7
N2 - 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.
AB - 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.
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U2 - 10.1128/JB.00172-11
DO - 10.1128/JB.00172-11
M3 - Article
C2 - 21602342
AN - SCOPUS:79960394966
VL - 193
SP - 3618
EP - 3623
JO - Journal of Bacteriology
JF - Journal of Bacteriology
SN - 0021-9193
IS - 14
ER -