Previous Article | Next Article 
Antimicrob Agents Chemother. 1985 May; 27(5): 791-797
Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.
J F Garcia-Bustos,
N Pezzi and
E Mendez
ABSTRACT
Microcin 7 is a small peptide produced and excreted to the culture medium by stationary-phase Escherichia coli cells harboring the pMccC7 plasmid (formerly named pRYC7). This peptide inhibited the growth of the enterobacteria phylogenetically closer to E. coli, apparently by blocking protein biosynthesis. The molecule was degraded with trypsin, and the resulting fragments were purified and sequenced. The results show that microcin 7 is a linear heptapeptide blocked at both ends.
Antimicrob Agents Chemother. 1985 May; 27(5): 791-797
This article has been cited by other articles:
-
Fomenko, D. E., Metlitskaya, A. Z., Peduzzi, J., Goulard, C., Katrukha, G. S., Gening, L. V., Rebuffat, S., Khmel, I. A.
(2003). Microcin C51 Plasmid Genes: Possible Source of Horizontal Gene Transfer. Antimicrob. Agents Chemother.
47: 2868-2874
[Abstract]
[Full Text]
-
Rodriguez, E., Lavina, M.
(2003). The Proton Channel Is the Minimal Structure of ATP Synthase Necessary and Sufficient for Microcin H47 Antibiotic Action. Antimicrob. Agents Chemother.
47: 181-187
[Abstract]
[Full Text]
-
Trujillo, M., Rodriguez, E., Lavina, M.
(2001). ATP Synthase Is Necessary for Microcin H47 Antibiotic Action. Antimicrob. Agents Chemother.
45: 3128-3131
[Abstract]
[Full Text]
-
Castle, M., Nazarian, A., Yi, S. S., Tempst, P.
(1999). Lethal Effects of Apidaecin on Escherichia coli Involve Sequential Molecular Interactions with Diverse Targets. J. Biol. Chem.
274: 32555-32564
[Abstract]
[Full Text]
-
Guijarro, J. Iña., González-Pastor, J. E., Baleux, F.ço., Millán, J. L. S., Castilla, M. A., Rico, M., Moreno, F., Delepierre, M.
(1995). Chemical Structure and Translation Inhibition Studies of the Antibiotic Microcin C7. J. Biol. Chem.
270: 23520-23532
[Abstract]
[Full Text]