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Gene Review

TTHA1893  -  S-layer P100 protein

Thermus thermophilus HB8

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Disease relevance of TTHA1893

  • After 48 hours of incubation at 70 degrees C, only two constructions that contained the kat gene flanked by Thermus sequences from both sides of slpA were able to produce protein layer (P100)-defective mutants [1].
  • Expression was apparently independent of Plac, indicating that the promoter for P100 is functional in E. coli [2].

High impact information on TTHA1893

  • DNA sequence analysis of the region upstream to the slpA gene revealed the presence of an open reading frame (ORF) which coded for a 604-amino-acid protein highly homologous to the glucosamine-6-P synthases (EC of both prokaryotic and eukaryotic origin [3].
  • The glmSth gene is transcribed divergently from slpA in a 2.0 kb mRNA which probably also includes a tryptophan tRNA gene (trpTth) identified at its 3' extreme [3].
  • As the products of both the glmSth and the slpA genes are main components of the cell envelope of T. thermophilus, their unusual clustering in the chromosome could be related to the existence of specific mechanisms for their coordinate expression [3].
  • The transcription and translation signals of the S-layer gene (slpA) from Thermus thermophilus HB8 have been used to express a thermostable kanamycin adenyl transferase gene in this organism [1].
  • The accessibility of the binding sites in hexagonal, trigonal, or tetragonal assemblies of P100 was analyzed by enzyme-linked immunosorbent assays with six of these MAbs and their respective Fab fragments [4].

Associations of TTHA1893 with chemical compounds

  • Removal of Ca2+ unstabilized the HMrPs, which dissociated into P100 when heated at 80 to 85 degrees C in 10% (wt/vol) sodium dodecyl sulfate, indicating that HMrPs were oligomeric complexes of P100 [5].

Analytical, diagnostic and therapeutic context of TTHA1893

  • We demonstrate here by limited proteolysis and Western blotting the surprising fact that the protein component of the three crystals is the P100 protein [6].


  1. Insertional mutagenesis in the extreme thermophilic eubacteria Thermus thermophilus HB8. Lasa, I., Castón, J.R., Fernández-Herrero, L.A., de Pedro, M.A., Berenguer, J. Mol. Microbiol. (1992) [Pubmed]
  2. Cloning and expression in Escherichia coli of the structural gene coding for the monomeric protein of the S layer of Thermus thermophilus HB8. Faraldo, M.L., de Pedro, M.A., Berenguer, J. J. Bacteriol. (1991) [Pubmed]
  3. glmS of Thermus thermophilus HB8: an essential gene for cell-wall synthesis identified immediately upstream of the S-layer gene. Fernández-Herrero, L.A., Badet-Denisot, M.A., Badet, B., Berenguer, J. Mol. Microbiol. (1995) [Pubmed]
  4. Differential domain accessibility to monoclonal antibodies in three different morphological assemblies built up by the S-layer protein of Thermus thermophilus HB8. Castón, J.R., Olabarría, G., Lasa, I., Carrascosa, J.L., Berenguer, J. J. Bacteriol. (1996) [Pubmed]
  5. Ca2+-stabilized oligomeric protein complexes are major components of the cell envelope of "Thermus thermophilus" HB8. Berenguer, J., Faraldo, M.L., de Pedro, M.A. J. Bacteriol. (1988) [Pubmed]
  6. S-layer protein from Thermus thermophilus HB8 assembles into porin-like structures. Castón, J.R., Berenguer, J., de Pedro, M.A., Carrascosa, J.L. Mol. Microbiol. (1993) [Pubmed]
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