Complete amino acid sequence of ribosomal protein S14 from Bacillus stearothermophilus and homology studies to other ribosomal proteins

FEBS Letters

Herfurth, Elke¹  Briesemeister, Ulrike¹  Wittmann-Liebold, Brigitte¹ 

[1] Max-Delbrück-Centrum für Molekulare Medizin, Abteilung Proteinchemie, Robert-Rössle-Straße 10, 13125 Berlin, Germany

关键词: Ribosomal protein;    Protein sequencing;    Evolution;    Bacillus stearothermophilus;    L-proteins;    large ribosomal subunit proteins;    PTH;    phenylthiohydantoin;    RP-HPLC;    reversed-phase high performance liquid chromatography;    rRNA;    ribosomal RNA;    S-proteins;    small ribosomal subunit proteins;    TFA;    trifluoroacetic acid;    tRNA;    transfer-RNA;   

DOI  :  10.1016/0014-5793(94)00838-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown