Structural and Functional Analysis of the S-Layer Protein from Bacillus stearothermophilus

  • Beatrix Kuen
  • Werner Lubitz
  • Geoffrey J. Barton
Part of the NATO ASI Series book series (NSSA, volume 252)


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).


Cell Wall Protein Bacillus Stearothermophilus Prokaryotic Species Protein Multiple Sequence Alignment Strain PV72 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Barton, G.J., 1990, Protein multiple sequence alignment and flexible pattern matching, Meth. Enzymol. 183: 403.PubMedCrossRefGoogle Scholar
  2. Barton, G.J., and Sternberg, M.J.E., 1987a, Evaluation and improvements in the automatic alignment of protein sequences, Prot. Engin. 1: 89.CrossRefGoogle Scholar
  3. Barton, G.J., and Sternberg, M.J.E., 1987b, A strategy for the rapid multiple alignment of protein sequences: confidence levels for tertiary structure comparisons, J. Mol. Biol. 198: 327.PubMedCrossRefGoogle Scholar
  4. Barton, G.J., and Sternberg, M.J.E., 1990, Flexible protein sequence patterns - a sensitive method to detect weak structural similarities, J. Mol. Biol. 212: 389.PubMedCrossRefGoogle Scholar
  5. Bowditch, R.D., Baumann, P., and Yousten, A.A., 1989, Cloning and sequencing of the gene encoding a 125-kilodalton surface-layer protein from Bacillus sphaericus 2362 and of a related cryptic gene, J. Bacteriol. 171: 4 1788.Google Scholar
  6. Ebisu, S., Tsuboi, A., Takagi, H., Naruse, Y., Yamagata, H., Tsukagoshi, N., and Udaka, S., 1990, Conserved structures of cell wall protein genes among protein-producing Bacillus brevis strains, J. Bacteriol. 172: 1312.PubMedGoogle Scholar
  7. Gamier, J., Osguthorpe, D.J., and Robson, B., 1978, Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins, J. Mol. Biol. 120: 97.CrossRefGoogle Scholar
  8. Gilmore, R.D., Joste, J.N., and McDonald, G.A., 1989, Cloning, expression and sequence analysis of the gene encoding the 120 kD surface-exposed protein of Rickettsia rickettsii, Mol. Microbiol. 3: 1579.PubMedCrossRefGoogle Scholar
  9. Gruber, K. and Sleytr, U.B., 1991, Influence of an S-layer on surface properties of Bacillus stearothermophilus, Arch. Microbiol. 156: 181.PubMedCrossRefGoogle Scholar
  10. Messner, P. and Sleytr, U. B., 1992, Crystalline bacterial cell-surface layers, Adv. Microbial Physiol., 33: 213.Google Scholar
  11. Messner, P., Hollaus, F., and Sleytr, U.B., 1984, Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains, Int. J. Syst. Bacteriol. 34: 202.CrossRefGoogle Scholar
  12. Pum, D., Sara, M., Messner, P., and Sleytr, U.B., 1991, Two-dimensional (glyco)protein crystals as pattering elements for the controlled immobilization of functional molecules, Nanotechnol. 2: 196.CrossRefGoogle Scholar
  13. Sleytr, U.B., Sara, M., Küpcü, Z., and Messner, P., 1986, Structural and chemical characterization of S-layers of selected strains of Bacillus stearothermophilus and Desulfotomaculum nigrificans, Arch. Microbiol. 146: 19.PubMedCrossRefGoogle Scholar
  14. Sleytr, U.B., Sara, M., and Pum,D., 1989, Application potentials of two dimensional protein crystals, Microelectr. Engin. 9: 13.CrossRefGoogle Scholar
  15. Smith, T.F., and Waterman, M.S., 1981, Identification of common molecular subsequences, J. Mol. Biol. 147: 195.PubMedCrossRefGoogle Scholar
  16. Tsuboi, A., Uchihi, R., Tabata, R., Takahashi, Y., Hashiba, H., Sasaki, T., Yamagata, H., Tsukagoshi, N., and Udaka, S., 1986, Characterization of the genes coding for two major cell wall proteins from protein-producing Bacillus brevis 47: complete nucleotide sequence of the outer wall protein gene, J. Bacteriol. 168: 365.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Beatrix Kuen
    • 1
  • Werner Lubitz
    • 1
  • Geoffrey J. Barton
    • 2
  1. 1.Institute of Microbiology and GeneticsUniversity of ViennaViennaAustria
  2. 2.Laboratory of Molecular BiophysicsUniversity of OxfordOxfordEngland

Personalised recommendations