Chemical structure and translation inhibition studies of the antibiotic microcin C7. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 1995

Chemical structure and translation inhibition studies of the antibiotic microcin C7.

Résumé

Escherichia coli microcin C7 (MccC7) is an antibiotic that inhibits protein synthesis in vivo. It is a heptapeptide containing unknown modifications at the N and C termini (Garc?Bustos, J. F., Pezzi, N., and M?ez, E. (1985) Antimicrob. Agents Chemoth. 27, 791-797). The chemical structure of MccC7 has been characterized by use of 1H homonuclear and heteronuclear (13C, 15N, 31P) nuclear magnetic resonance spectroscopy as well as mass spectrometry (1177 +/- 1 Da). The heptapeptide Met-Arg-Thr-Gly-Asn-Ala-Asp is substituted at the N terminus by a N-formyl group. The C-terminal substituent consists of the phosphodiester of 5'-adenylic acid and n-aminopropanol (AMPap), which is linked via the phosphorus atom to an amide group, thus forming a phosphoramide. The main chain carbonyl of the C-terminal aspartic acid residue is connected via this amide bond to the modified nucleotide unit. MccC7 and the peptide unit inhibit protein translation in vitro while a synthetic analog of the AMPap substituent is not active. Neither the peptide nor the AMPap molecule has an effect on the growth of MccC7-sensible cells. Our results strongly suggest that the peptide is responsible for MccC7 antibiotic activity while the C-terminal substituent is needed for MccC7 transport. Implications of the structure determined in this work for MccC7 synthesis and mode of action are discussed.
Fichier sous embargo
Fichier sous embargo
Date de visibilité indéterminée

Dates et versions

pasteur-00364887 , version 1 (27-02-2009)

Identifiants

Citer

J. I. Guijarro, J. E. González-Pastor, F. Baleux, J. L. San Millán, M. A. Castilla, et al.. Chemical structure and translation inhibition studies of the antibiotic microcin C7.. Journal of Biological Chemistry, 1995, 270 (40), pp.23520-32. ⟨10.1074/jbc.270.40.23520⟩. ⟨pasteur-00364887⟩

Collections

PASTEUR CNRS
50 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More