Complete amino acid sequence of ribosomal protein S14 from Bacillus stearothermophilus and homology studies to other ribosomal proteins.
The complete amino acid sequence of protein S14 from the small subunit of Bacillus stearothermophilus was determined by N-terminal sequence analysis and by sequencing of overlapping peptides obtained from enzymatic digestions. Protein S14 consists of 60 amino acid residues with a molecular mass of 7148 Da. It has a high content of basic amino acids and a predicted isoelectric point of 11.46. Protein S14 contains two pairs of cysteines in the carboxyl-terminal region, presumably linked by two sulphur bridges. A comparison between protein S14 of B. stearothermophilus and homologous proteins from other organisms revealed highly conserved carboxyl-termini for this protein in eubacteria, archaebacteria and eukaryotes.
Herfurth
E
E
Max-Delbrück-Centrum für Molekulare Medizin, Abteilung Proteinchemie, Berlin, Germany.
Briesemeister
U
U
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid
D012269:Ribosomal Proteins; C039747:ribosomal protein S14