Proteomic analysis of the bacteriocin thuricin 17 produced by Bacillus thuringiensis NEB17

FEMS Microbiol Lett. 2006 Feb;255(1):27-32. doi: 10.1111/j.1574-6968.2005.00054.x.

Abstract

Thuricin 17 is a recently discovered bacteriocin produced by Bacillus thuringiensis NEB17. The objective of this work was to conduct a proteomic analysis of this bacteriocin. The partial N- and C-terminal amino-acid sequences of thuricin 17 have now been determined using the Edman degradation and matrix-assisted laser desorption ionization-quadrapole time of flight mass spectrometry (MS)/MS. A hydrophobic cluster analysis indicates that thuricin 17 contains a hydrophobic region, potentially corresponding to a membrane associated domain. Based on time of production, this bacteriocin may be produced as a secondary metabolite. Interestingly, thuricin 17 shares the same N-terminal sequence, DWTXWSXL, with a previously reported bacteriocin, Bacthuricin F4, produced by B. thuringiensis ssp. kurstaki strain BUPM4. This is the first time two bacteriocins from different Bacillus species have been shown to share similar N-terminal sequences.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus thuringiensis / genetics
  • Bacillus thuringiensis / growth & development
  • Bacillus thuringiensis / metabolism*
  • Bacteriocins / biosynthesis
  • Bacteriocins / chemistry*
  • Bacteriocins / isolation & purification*
  • Bacteriocins / metabolism
  • Proteomics
  • Sequence Analysis, Protein

Substances

  • Bacteriocins
  • thuricin