The N-terminal sequence of ribosomal protein L10 from the archaebacterium Halobacterium marismortui and its relationship to eubacterial protein L6 and other ribosomal proteins

Biol Chem Hoppe Seyler. 1987 Aug;368(8):921-5. doi: 10.1515/bchm3.1987.368.2.921.

Abstract

The amino-terminal sequence of ribosomal protein L10 from Halobacterium marismortui has been determined up to residue 54, using both a liquid- and a gas-phase sequenator. The two sequences are in good agreement. The protein is clearly homologous to protein HcuL10 from the related strain Halobacterium cutirubrum. Furthermore, a weaker but distinct homology to ribosomal protein L6 from Escherichia coli and Bacillus stearothermophilus can be detected. In addition to 7 identical amino acids in the first 36 residues in all four sequences a number of conservative replacements occurs, of mainly hydrophobic amino acids. In this common region the pattern of conserved amino acids suggests the presence of a beta-alpha fold as it occurs in ribosomal proteins L12 and L30. Furthermore, several potential cases of homology to other ribosomal components of the three ur-kingdoms have been found.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / analysis
  • Halobacterium / analysis*
  • Ribosomal Protein L10
  • Ribosomal Proteins / analysis*

Substances

  • Ribosomal Proteins
  • ribosomal protein L6