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Gewählte Publikation:

Kuen, B; Sleytr, UB; Lubitz, W.
(1994): Sequence analysis of the sbsA gene encoding the 130-kDa surface-layer protein of Bacillus stearothermophilus strain PV72.
Gene. 1994; 145(1):115-120

Bacillus stearothermophilus (Bs) contains a surface-layer (S-layer) protein (SbsA), which forms a hexagonal array on the cell wall. In order to understand the structural/functional relationship of SbsA from Bs PV72, the entire nucleotide (nt) sequence of the sbsA gene was determined from three overlapping fragments. The 3'-end was cloned and expressed in Escherichia coli, whereas the 5'-region was amplified from the genome of Bs PV72 by the polymerase chain reaction using two overlapping fragments. The open reading frame (3684 nt) of sbsA is predicted to encode a protein of 1228 amino acids (aa). The SbsA is synthesized with a leader sequence of 30 aa. The predicted SbsA aa profile was similar to most other sequenced S-layer proteins, containing more acidic than basic aa (pI 5.1) and a very low amount of sulfur-containing aa. Based on aa sequence data, SbsA has weak homology of with the S-layer proteins from B. sphaericus, Rickettsia rickettsii, B. brevis HPD31 and B. brevis 47 (OWP).
Autor*innen der BOKU Wien:
Sleytr Uwe B.
Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Bacterial Outer Membrane Proteins - genetics
Bacterial Proteins -
Base Sequence -
Cloning, Molecular -
DNA, Bacterial -
Genes, Bacterial -
Geobacillus stearothermophilus - genetics
Membrane Proteins -
Molecular Sequence Data -
Open Reading Frames -
Polymerase Chain Reaction -
Restriction Mapping -
Sequence Homology, Amino Acid -

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