The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus

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Abstract
The amino acid sequences of ribosomal proteins L1, L14, L15, L23, L24 and L29 from B. stearothermophilus have been completely determined. This was achieved by sequence analyses of peptides derived from enzymatic digestion of the proteins with trypsin, chymotrypsin, pepsin, Staphylococcus aureus protease, Armillaria mellea protease and by chemical cleavage with hydroxylamine and cyanogen bromide. Based on the primary structures of the 6 proteins, their secondary structures were predicted using 4 different computer prediction programs. A comparison of the amino acid sequences of the studied proteins from B. stearothermophilus with the homologous proteins from Escherichia coli revealed that in 4 proteins (L1, L15, L24 and L29) between 40-50% of the residue in the sequences are identical, whereas this value is significantly higher (69%) for L14 and lower (28%) for L23. The distribution of those amino acid residues which are identical in the corresponding proteins from the 2 bacteria is not random along the protein chain: some regions are highly conserved whereas others are not. This finding indicates that the regions which are conserved during evolution are important for the spatial structure and/or function of the protein.