The N-terminal sequence of ribosomal protein L10 from the archaebacterium Halobacterium marismortui and its relationship to eubacterial protein L6 and other ribosomal proteins.
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.
Dijk
J
J
Max-Plank-Institut für Molekulare Genetik, Abt. Wittmann, Berlin.
van den Broek
R
R
Nasiulas
G
G
Beck
A
A
Reinhardt
R
R
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000032:analysis; D006217:Halobacterium / Q000032:analysis*; D000080882:Ribosomal Protein L10; D012269:Ribosomal Proteins / Q000032:analysis*
D012269:Ribosomal Proteins; C031249:ribosomal protein L6