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The complete amino acid sequence of ribosomal protein S18 from the moderate thermophile Bacillus stearothermophilus
Author(s) -
McDougall John,
Choli Theodora,
Kruft Volker,
Kapp Ulrike,
Wittmann-Liebold Brigitte
Publication year - 1989
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(89)80232-7
Subject(s) - cyanogen bromide , ribosomal protein , peptide sequence , biochemistry , thermophile , amino acid , chemistry , homology (biology) , protease , ribosomal rna , biology , enzyme , ribosome , gene , rna
The amino acid sequence of ribosomal protein S18 from Bacillus stearothermophilus has been completely determined by automated sequence analysis of the intact protein as well as of peptides derived from digestion with Staphylococcus aureus protease at pH 4.0 and cleavage with cyanogen bromide. The carboxy‐terminal region was verified by both amino acid analyses of chymotryptic peptides and by mass spectrometry from the terminal region. The protein contains 77 amino acid residues and has an M r of 8838. Comparison of this sequence with the sequences of the S18 proteins from tobacco and liverwort chloroplasts and E. coli shows a relatively high similarity, ranging from 42 to 55% identical residues with the B. stearothermophilus S18 protein. The regions of homology common to all four proteins consist of several positively charged sections spanning the entire length of the protein.