An Acidic, Alanine-rich 50 S Ribosomal Protein from 'Halobacterium cutirubrum': Amino Acid Sequence Homology with 'Escherichia coli' Proteins L7 and L12,
NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES
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The 50 S ribosomal subunits from H. cutirubrum contain an alanine-rich, acidic protein L20. Its high alanine content over 25, its acidity and its lack of histidine, cysteine and tryptophan residues make this protein a possible equivalent to the only sequenced 50 S ribosomal protein L7L12 of E. coli. A large tryptic peptide L20-T4, which belongs to the carboxyl-terminal half of the protein, has been isolated from H. cutirubrum L20. The amino-terminal regions of L20 and of peptide L20-T4 have been sequenced. The results indicate a high degree of homology of the first 30 residues of L20 with the central region of E. coli L7L12 and the first 15 residues of L20-T4 with the carboxyl-terminal region of E. coli L7L12.