title: Proteomic analysis of the bacteriocin thuricin 17 produced by Bacillus thuringiensis NEB17.
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.
authors.affiliation: Department of Plant Science, McGill University, St. Anne-de-Bellevue, QC, Canada.
authors.forename: Elizabeth J
authors.initials: EJ
authors.lastname: Gray
authors.forename: Marcos
authors.initials: M
authors.lastname: Di Falco
authors.forename: Alfred
authors.initials: A
authors.lastname: Souleimanov
authors.forename: Donald L
authors.initials: DL
authors.lastname: Smith
mesh_terms: D001413:Bacillus thuringiensis / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D040901:Proteomics; D020539:Sequence Analysis, Protein
chemical_list: D001430:Bacteriocins; C059740:thuricin