The amino-acid sequences of the Bacillus stearothermophilus ribosomal proteins S17 and S21 and their comparison to homologous proteins of other ribosomes.
Ribosomal proteins S17 and S21 from the moderate thermophile Bacillus stearothermophilus were purified by one-step high-performance liquid chromatography from the 30S-subunit protein mixture employing a semi-preparative reversed-phase C4 column. The complete amino-acid sequences of these proteins were determined by a combination of N-terminal sequencing in picomole quantities of the protein and of appropriate peptide fragments. Proteins S17 and S21 consist of 86 and 55 amino-acid residues, corresponding to molecular masses of 10074 and 6593 Da, respectively. They are homologous to proteins S17 and S21 from the Escherichia coli ribosome, showing 50 and 55% identities in the corresponding regions, respectively. The C-terminal region of protein S21 from B. stearothermophilus has a deletion of 15 residues as compared to the E. coli S21 protein. The evolutionary relationships of the Bacillus proteins to various other members of the S17 and S21 ribosomal protein families are discussed.
Herfurth
E
E
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin-Dahlem.
Hirano
H
H
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D012269:Ribosomal Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C037084:ribosomal protein S17; C032643:ribosomal protein S21