Megacinogenic plasmids of Bacillus megaterium

Tersch, M A Von; Carlton, Bruce C.

doi:10.1128/jb.155.2.872-877.1983

Cited by 39 publications

(13 citation statements)

References 31 publications

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“…Both megacins show phospholipase A2 activity, involved in converting phospholipids to the corresponding lysophospholipids (Von Tersch & Carlton, 1983a). Both structural and immunity genes of megacins A-216 and A-19213 are plasmid encoded on pBM309 (48 kb) and pBM113 (44 kb) in the B. megaterium 216 and ATCC 19213 strains, respectively (Rostas et al, 1980;Von Tersch & Carlton, 1983b). Megacin A-216 contains 293 amino acid residues and shows a native molecular weight of c. 66 kDa (Kiss et al, 2008).…”

Section: Class III Large Proteinsmentioning

confidence: 99%

Diversity and applications ofBacillusbacteriocins

et al. 2011

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Members of the genus Bacillus are known to produce a wide arsenal of antimicrobial substances, including peptide and lipopeptide antibiotics, and bacteriocins. Many of the Bacillus bacteriocins belong to the lantibiotics, a category of post-translationally modified peptides widely disseminated among different bacterial clades. Lantibiotics are among the best-characterized antimicrobial peptides at the levels of peptide structure, genetic determinants and biosynthesis mechanisms. Members of the genus Bacillus also produce many other nonmodified bacteriocins, some of which resemble the pediocin-like bacteriocins of the lactic acid bacteria (LAB), while others show completely novel peptide sequences. Bacillus bacteriocins are increasingly becoming more important due to their sometimes broader spectra of inhibition (as compared with most LAB bacteriocins), which may include Gram-negative bacteria, yeasts or fungi, in addition to Gram-positive species, some of which are known to be pathogenic to humans and/or animals. The present review provides a general overview of Bacillus bacteriocins, including primary structure, biochemical and genetic characterization, classification and potential applications in food preservation as natural preservatives and in human and animal health as alternatives to conventional antibiotics. Furthermore, it addresses their environmental applications, such as bioprotection against the pre- and post-harvest decay of vegetables, or as plant growth promoters.

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Section: Class III Large Proteinsmentioning

confidence: 99%

Diversity and applications ofBacillusbacteriocins

et al. 2011

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“…Endpoint sensitivity was determined as the reciprocal of the highest dilution that inhibited the growth of the indicator bacteria by at least 50%. The indicator strains are described in the accompanying paper (23). the megacin they produce, but were significantly more sensitive to the other megacin.…”

Section: Resultsmentioning

confidence: 99%

“…These strains were, respectively, 100-and 20-fold more sensitive to megacin A-216 than strain 216, yet showed approximately the same sensitivity to megacin A-19213 as strain 216. Strain VT1206 (a cured derivative of ATCC 19213 [23]) was 10 times more sensitive to megacin A-19213 than its parent strain, yet somewhat less sensitive to megacin A-216 than its parent strain.…”

Section: Resultsmentioning

confidence: 99%

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Bacteriocin from Bacillus megaterium ATCC 19213: comparative studies with megacin A-216

Tersch¹,

Carlton²

1983

J Bacteriol

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A bacteriocin produced by Bacillus megaterium ATCC 19213 was identified, purified, and compared with megacin A from B. megaterium 216. The ATCC 19213 bacteriocin was inducible with mitomycin C and showed phospholipase A activity. Both megacin A-216 and megacin A-19213 contained two dissimilar polypeptide subunits. Megacin A-216 contains a 30,000-dalton (x subunit and a 15,000-dalton ,B subunit. Megacin A-19213 is composed of an cx subunit 18,000 daltons in mass and a ,B subunit about 7,500 daltons in mass. No sequence similarities between ot and a subunits of either megacin were detected. The two megacins were further distinguished by quantitative differences in activity spectra and by immunodiffusion analyses. the method of Lowry et al. (16).Protoplast lysis by megacins. Indicator strain B. megaterium 2165 was grown to mid-logarithmic phase in yeast extract-tryptone broth at 37°C. Cells were pelleted by centrifugation and then resuspended in 20% sucrose-50 mM NaPO4, pH 7.0 (PS buffer), 866 on August 5, 2020 by guest

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“…Antibacterial proteins are a class of very important proteins that exist widely in the bodies or secretions of plants (Roberts & Selitrennikoff, 1986), microorganisms (Von Tersch & Carlton, 1983), insects (Okada & Natori, 1985) and animals (Scheit et al, 1985). Liu et al (1990) screened and isolated a B. subtilis strain (named A014) whose secretions possess very strong antibacterial activities, especially against the pathogen (Xanthomonas campestris pv.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCI expressed inEscherichia coli

Zhu

Chen

Gong

et al. 2001

Acta Crystallogr D Biol Cryst

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LCI is a type of novel antibacterial polypeptide secreted by a Bacillus subtilis strain. It consists of 47 residues with a molecular weight of 5468 Da. Using bioengineering, LCI was expressed in Escherichia coli DH5 with recombinant plasmid pBVAB16. It was crystallized using PEG 4000 as a precipitant. The crystal belongs to space group P6 2 22 or P6 4 22, with unit-cell parameters a = b = 29.30, c = 187.09 A Ê , and diffracts to 2.44 A Ê . A set of diffraction data to 2.8 A Ê was collected.

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Megacinogenic plasmids of Bacillus megaterium

Cited by 39 publications

References 31 publications

Diversity and applications ofBacillusbacteriocins

Diversity and applications ofBacillusbacteriocins

Bacteriocin from Bacillus megaterium ATCC 19213: comparative studies with megacin A-216

Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCI expressed inEscherichia coli

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