The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui.
The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13,538, 16,812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.
Hatakeyama
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Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
Hatakeyama
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Kimura
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D000595:Amino Acid Sequence; D000814:Aniline Compounds; D019843:Archaeal Proteins; D005075:Biological Evolution; D029968:Escherichia coli Proteins; D006217:Halobacterium / Q000235:genetics*; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000235:genetics*; D012995:Solubility
D000814:Aniline Compounds; D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; C027937:ribosomal protein L16; C043816:ribosomal protein L23, E coli; C489051:ribosomal protein L33, archaea; C489052:rpmG protein, E coli; C487557:4-trifluoromethylaniline