The complete amino acid sequence of ribosomal protein S18 from the moderate thermophile Bacillus stearothermophilus

FEBS Lett. 1989 Mar 13;245(1-2):253-60. doi: 10.1016/0014-5793(89)80232-7.

Abstract

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 Mr 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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Chloroplasts / analysis
  • Chromatography, High Pressure Liquid
  • Chymotrypsin
  • Escherichia coli / analysis
  • Geobacillus stearothermophilus / analysis*
  • Metalloendopeptidases
  • Molecular Sequence Data
  • Peptide Fragments
  • Protein Conformation
  • Ribosomal Proteins* / analysis
  • Sequence Homology, Nucleic Acid

Substances

  • Amino Acids
  • Peptide Fragments
  • Ribosomal Proteins
  • ribosomal protein S18
  • Chymotrypsin
  • Metalloendopeptidases
  • auR protein, Staphylococcus aureus