Autolysis of Cell Walls of Bacillus Subtilis. Mechanism and Possible Relationship to Competence.
نویسندگان
چکیده
منابع مشابه
Biochemical Aspects of Competence in the Bacillus Subtilis Transformation System. Ii. Autolytic Enzyme Activity of Cell Walls.
A lytic factor, associated with the cell wall, was fortuitously discovered during the course of the investigations described in the previous paper (1). In the pneumococcal transformation system (2-5) as well as in the Bacillus subtilis transformation system (6), the highly transformable strains possessed active autolytic enzymes. Consequently, studies were undertaken to investigate the relation...
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The structure of peptidoglycans of Escherichia coli and Bacillus subtilis is similar except for a few minor modifications, but murein (cell wall) structures are extremely different because the major cell wall constituents, anionic polymers, are not attached to peptidoglycans of E. coli but are attached to those of B. subtilis. Thickness of the cell walls in B. subtilis and the presence of an ou...
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In contrast to many nanotoxicity studies where nanoparticles (NPs) are observed to be toxic or reduce viable cells in a population of bacteria, we observed that increasing concentration of TiO2 NPs increased the cell survival of Bacillus subtilis in autolysis-inducing buffer by 0.5 to 5 orders of magnitude over an 8 hour exposure. Molecular investigations revealed that TiO2 NPs prevent or delay...
متن کاملBiochemical Aspects of Competence in the Bacillus subtilis Transformation System
A lytic factor, associated with the cell wall, was fortuitously discovered during the course of the investigations described in the previous paper (1). In the pneumococcal transformation system (2-5) as well as in the Bacillus subtilis transformation system (6), the highly transformable strains possessed active autolytic enzymes. Consequently, studies were undertaken to investigate the relation...
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Bacillus subtilis cell wall-bound protein CWBP33 is encoded by lytE, a gene expressed during the exponential growth phase. Sequence analysis of LytE, a 33-kDa protein, reveals two domains. The N-terminal domain contains a threefold-repeated motif common to several peptidoglycan binding proteins, while the C-terminal domain, probably carrying the catalytic activity, has homology with certain exo...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 239 شماره
صفحات -
تاریخ انتشار 1964