Biochemical and Genetic Characterization of Coagulin, a New Antilisterial Bacteriocin in the Pediocin Family of Bacteriocins, Produced by Bacillus coagulans I 4
- 1 December 2000
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 66 (12), 5213-5220
- https://doi.org/10.1128/aem.66.12.5213-5220.2000
Abstract
A plasmid-linked antimicrobial peptide, named coagulin, produced byBacillus coagulans I4 has recently been reported (B. Hyronimus, C. Le Marrec and M. C. Urdaci, J. Appl. Microbiol. 85:42–50, 1998). In the present study, the complete, unambiguous primary amino acid sequence of the peptide was obtained by a combination of both N-terminal sequencing of purified peptide and the complete sequence deduced from the structural gene harbored by plasmid I4. Data revealed that this peptide of 44 residues has an amino acid sequence similar to that described for pediocins AcH and PA-1, produced by different Pediococcus acidilacticistrains and 100% identical. Coagulin and pediocin differed only by a single amino acid at their C terminus. Analysis of the genetic determinants revealed the presence, on the pI4 DNA, of the entire 3.5-kb operon of four genes described for pediocin AcH and PA-1 production. No extended homology was observed between pSMB74 fromP. acidilactici and pI4 when analyzing the regions upstream and downstream of the operon. An oppositely oriented gene immediately dowstream of the bacteriocin operon specifies a 474-amino-acid protein which shows homology to Mob-Pre (plasmid recombination enzyme) proteins encoded by several small plasmids extracted from gram-positive bacteria. This is the first report of a pediocin-like peptide appearing naturally in a non-lactic acid bacterium genus.Keywords
This publication has 95 references indexed in Scilit:
- The mobilization protein, MobM, of the streptococcal plasmid pMV158 specifically cleaves supercoiled DNA at the plasmid oriTJournal of Molecular Biology, 1997
- Biosynthesis of bacteriocins in lactic acid bacteriaAntonie van Leeuwenhoek, 1996
- Maturation pathway of nisin and other lantibiotics: post‐translationally modified antimicrobial peptides exported by Gram‐positive bacteriaMolecular Microbiology, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilacticiJournal of Applied Bacteriology, 1993
- Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroidesJournal of General Microbiology, 1992
- Purification, characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus acidilacticiJournal of Applied Bacteriology, 1988
- Analysis of membrane and surface protein sequences with the hydrophobic moment plotJournal of Molecular Biology, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Calcium-dependent bacteriophage DNA infectionJournal of Molecular Biology, 1970