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Complete amino acid sequence of ribosomal protein S14 from Bacillus stearothermophilus and homology studies to other ribosomal proteins
Author(s) -
Herfurth Elke,
Briesemeister Ulrike,
Wittmann-Liebold Brigitte
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00838-8
Subject(s) - ribosomal protein , biochemistry , amino acid , peptide sequence , biology , homology (biology) , isoelectric point , protein subunit , ribosomal rna , microbiology and biotechnology , ribosome , enzyme , gene , rna
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.