Abstract
One feature common to many bacteria, regardless of their phylogenetic origin within the kingdoms Eucarya or Archaea, is the presence of a regularly ordered (glyco)protein border as the outermost macromolecular layer of the cell envelope. A recent list of organisms with such crystalline surface layers (S-layers) cites approximately 300 different prokaryotic species (Messner and Sleytr, 1992). However, most of the S-layers have only been described by electron microscopical or biochemical investigations and DNA sequence data of the corresponding genes are available for very few species (approximately 20). Here we report on the structural and functional properties of the S-layer of Bacillus stearothermophilus strain PV72 which have been deduced from computer analysis of DNA-sequence data (for sequencing details of the gene see the contribution by Kuen, Sára, Sleytr, and Lubitz in this book).
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© 1993 Springer Science+Business Media New York
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Kuen, B., Lubitz, W., Barton, G.J. (1993). Structural and Functional Analysis of the S-Layer Protein from Bacillus stearothermophilus . In: Beveridge, T.J., Koval, S.F. (eds) Advances in Bacterial Paracrystalline Surface Layers. NATO ASI Series, vol 252. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9032-0_14
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DOI: https://doi.org/10.1007/978-1-4757-9032-0_14
Publisher Name: Springer, Boston, MA
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