Skip to main content
NCBI home page
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1985 May;27(5):791–797. doi: 10.1128/aac.27.5.791

Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.

J F Garcia-Bustos, N Pezzi, E Mendez
PMCID: PMC180153  PMID: 2861788

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.

Full text

PDF
791

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Asensio C., Pérez-Díaz J. C. A new family of low molecular weight antibiotics from enterobacteria. Biochem Biophys Res Commun. 1976 Mar 8;69(1):7–14. doi: 10.1016/s0006-291x(76)80264-1. [DOI] [PubMed] [Google Scholar]
  2. Baquero F., Bouanchaud D., Martinez-Perez M. C., Fernandez C. Microcin plasmids: a group of extrachromosomal elements coding for low-molecular-weight antibiotics in Escherichia coli. J Bacteriol. 1978 Aug;135(2):342–347. doi: 10.1128/jb.135.2.342-347.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berger E. A., Heppel L. A. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. J Biol Chem. 1974 Dec 25;249(24):7747–7755. [PubMed] [Google Scholar]
  4. Bornstein P. Structure of alpha-1-CB8, a large cyanogen bromide produced fragment from the alpha-1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides. Biochemistry. 1970 Jun 9;9(12):2408–2421. doi: 10.1021/bi00814a004. [DOI] [PubMed] [Google Scholar]
  5. Davis B. D., Tai P. C. The mechanism of protein secretion across membranes. Nature. 1980 Jan 31;283(5746):433–438. doi: 10.1038/283433a0. [DOI] [PubMed] [Google Scholar]
  6. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  7. Fitton J. E., Dell A., Shaw W. V. The amino acid sequence of the delta haemolysin of Staphylococcus aureus. FEBS Lett. 1980 Jun 30;115(2):209–212. doi: 10.1016/0014-5793(80)81170-7. [DOI] [PubMed] [Google Scholar]
  8. García-Bustos J. F., Pezzi N., Asensio C. Microcin 7: purification and properties. Biochem Biophys Res Commun. 1984 Mar 15;119(2):779–785. doi: 10.1016/s0006-291x(84)80318-6. [DOI] [PubMed] [Google Scholar]
  9. Guarente L. P., Isberg R. R., Syvanen M., Silhavy T. J. Conferral of transposable properties to a chromosomal gene in Escherichia coli. J Mol Biol. 1980 Aug 15;141(3):235–248. doi: 10.1016/0022-2836(80)90179-5. [DOI] [PubMed] [Google Scholar]
  10. Guyer R. L., Todd C. W. Protein sequencing: thermal conversion of thiazolinone derivatives of amino acids to thiohydantoins. Anal Biochem. 1975 Jun;66(2):400–404. doi: 10.1016/0003-2697(75)90607-7. [DOI] [PubMed] [Google Scholar]
  11. Ishiguro E. E., Ramey W. D. Stringent control of peptidoglycan biosynthesis in Escherichia coli K-12. J Bacteriol. 1976 Sep;127(3):1119–1126. doi: 10.1128/jb.127.3.1119-1126.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Laland S. G., Zimmer T. L. The protein thiotemplate mechanism of synthesis for the peptide antibiotics produced by Bacillus brevis. Essays Biochem. 1973;9:31–57. [PubMed] [Google Scholar]
  13. Mendez E., Lai C. Y. Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975 Sep;68(1):47–53. doi: 10.1016/0003-2697(75)90677-6. [DOI] [PubMed] [Google Scholar]
  14. NAUGHTON M. A., SANGER F., HARTLEY B. S., SHAW D. C. The amino acid sequence around the reactive serine residue of some proteolytic enzymes. Biochem J. 1960 Oct;77:149–163. doi: 10.1042/bj0770149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Perez-Diaz J. C., Clowes R. C. Physical characterization of plasmids determining synthesis of a microcin which inhibits methionine synthesis in Escherichia coli. J Bacteriol. 1980 Mar;141(3):1015–1023. doi: 10.1128/jb.141.3.1015-1023.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. SCHROEDER W. A., SHELTON J. R., SHELTON J. B., CORMICK J., JONES R. T. THE AMINO ACID SEQUENCE OF THE GAMMA CHAIN OF HUMAN FETAL HEMOGLOBIN. Biochemistry. 1963 Sep-Oct;2:992–1008. doi: 10.1021/bi00905a016. [DOI] [PubMed] [Google Scholar]
  17. Savige W. E., Fontana A. Interconversion of methionine and methionine sulfoxide. Methods Enzymol. 1977;47:453–459. doi: 10.1016/0076-6879(77)47045-9. [DOI] [PubMed] [Google Scholar]
  18. Spiess J., Rivier J., Rivier C., Vale W. Primary structure of corticotropin-releasing factor from ovine hypothalamus. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6517–6521. doi: 10.1073/pnas.78.10.6517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tarr G. E., Beecher J. F., Bell M., McKean D. J. Polyquarternary amines prevent peptide loss from sequenators. Anal Biochem. 1978 Feb;84(2):622–7?0=ENG. doi: 10.1016/0003-2697(78)90086-6. [DOI] [PubMed] [Google Scholar]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES