| | 1 | Author
| Stefan Antohi | Requires cookie* | | | Title
| Polycation-Bacterium Interactions and Wall Subunits as Endocytosis Factors. Topoisomeraselike Action of Basic Polypeptides Suggesting a 7th Class of Enzymes: The Stereases  | | | | Abstract
| Lysine rich histone and polylysine are bacteriolytic for Bacillus subtilis and Escherichia coli cells, whereas histones H2A, H2B and H3, assayed separately are not. Polyarginine bacteriolysis of E. coli with polycation 10 ug/ml decreased with higher concentrations, the killed nonlysed cells exhibiting wall alterations. All bacteriolytic polycations were lytically effective under reciprocal shaking, but not under magnetic stirring conditions, demonstrating the requirement for cell lysis of mechanical fields developed in oscillatory movements. Scanning electron microscopy o f histone HI treated B. subtilis cells showed the formation of globular bodies (polionosomes) in the cell surface. The interference of Ca2+ and 0 °C exposure with the polycation action observed especially in E. coli, the polionosomes, and the dynamics in polycationic cell lysis, considered together, suggest the existence o f wall supramolecular subunits (murameres), defined by their ability to form polionosomes. The murameres undergoing reversible conformational transitions induced by ectobiological signals, e.g., Ca2+, would make up an uptake system. The involvement of this system in environmental interactions and D N A uptaking, as well as the general stereo-enzyme like nature o f the conformational changes caused by polycations are discussed. | | | |
Reference
| Z. Naturforsch. 37c, 985—9 (1982); received December 10 1981/April 14 1982 | | | |
Published
| 1982 | | | |
Keywords
| Polionosome, Muramere, Sterease, Ca2+, Uptaking System | | | |
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| default:Reihe_C/37/ZNC-1982-37c-0985.pdf | | | | Identifier
| ZNC-1982-37c-0985 | | | | Volume
| 37 | |
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