Structural and Functional Analysis of the S-Layer Protein from Bacillus stearothermophilus
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).
KeywordsCell Wall Protein Bacillus Stearothermophilus Prokaryotic Species Protein Multiple Sequence Alignment Strain PV72
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- 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
- Messner, P. and Sleytr, U. B., 1992, Crystalline bacterial cell-surface layers, Adv. Microbial Physiol., 33: 213.Google Scholar
- 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