Author:
Austin John W.,Murray R. G. E.
Abstract
The regularly structured (RS) layer of Lampropedia hyalina was found to consist of two components; of these, the inner perforate layer was easily isolated from cell envelopes by dissolution of attached material by incubation in 2% sodium dodecyl sulfate at room temperature. The layer consisted of a 31.5-kilodalton polypeptide arranged in p6 symmetry so that, in negative stain, it appeared to be a sheet full of regularly arranged holes with a repeat frequency of 13 nm. The layer was stable in chelating and reducing agents, and in various detergents. Dissolution of the perforate layer occurred in boiling sodium dodecyl sulfate, 6 M guanidine–HCl, 8 M urea, 90% formic acid, and in buffers below pH 4 and above pH 11. In its dissociated state, the component polypeptide was sensitive to hydrolysis by endoproteinase glu-C, while the assembled polypeptide was not affected, suggesting that the acidic amino acid residues are hidden from the protease in the assembled state.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
9 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Lampropedia;Bergey's Manual of Systematics of Archaea and Bacteria;2015-09-14
2. Cell Fractionation;Methods for General and Molecular Microbiology;2014-04-30
3. Occurrence, Location, Ultrastructure and Morphogenesis of S-Layers;Crystalline Bacterial Cell Surface Proteins;1996
4. Crystalline Bacterial Cell-Surface Layers;Advances in Microbial Physiology Volume 33;1992
5. Antigenic differences among Campylobacter fetus S-layer proteins;Journal of Bacteriology;1990-09