Abstract
Crystalline inclusions were discovered in stationary and sporulating cells of the spore-forming bacterium Bacillus licheniformis ATCC 9945a. As detected by electron microscopy, dying or sporulating bacterial cells contain a single crystal of strikingly large size. The crystals in sporulating cells are located next to nascent spores and can be several times larger than the spores. Morphologically, most crystals are rhomboid with uniformly spaced grids. These newly discovered crystalline inclusions of B. licheniformis closely resemble parasporal crystals of Bacillus thuringiensis that are formed by insecticidal toxin proteins and used widely as biopesticides. The taxonomic identity of this strain was verified by its 16S rRNA gene sequence and its fatty acid profile. The finding of crystal proteins in B. licheniformis may lead to the discovery of new protein toxins and may expand our pool of biopesticides.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacillus / chemistry
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Bacillus / classification
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Bacillus / genetics
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Bacillus / ultrastructure*
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Bacillus thuringiensis Toxins
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Bacterial Toxins / chemistry
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Bacterial Toxins / genetics
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Bacterial Toxins / metabolism*
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Base Sequence
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Crystallization
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Endotoxins / chemistry
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Endotoxins / genetics
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Endotoxins / metabolism*
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Fatty Acids / analysis
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Hemolysin Proteins / chemistry
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Hemolysin Proteins / genetics
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Hemolysin Proteins / metabolism*
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Inclusion Bodies / chemistry
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Inclusion Bodies / metabolism
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Inclusion Bodies / ultrastructure*
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Microscopy, Electron
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RNA, Ribosomal, 16S / genetics
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Sequence Analysis, DNA
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Spores, Bacterial / metabolism
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Spores, Bacterial / ultrastructure
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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Endotoxins
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Fatty Acids
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Hemolysin Proteins
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RNA, Ribosomal, 16S
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insecticidal crystal protein, Bacillus Thuringiensis