Carboxyl-terminal sequences of procaryotic ribosomal proteins from Escherichia coli, Bacillus stearothermophilus, and Halobacterium cutirubrum.
The carboxyl-terminal amino acid sequences of two ribosomal proteins, Escherichia coli L12 and E. coli S4, and the proteins believed to be their equivalents from Bacillus stearothermophilus and Halobacterium cutirubrum, were determined. These proteins are known to be required for peptide chain termination (L12) and in ribosome assembly (S4). The carboxyl-terminal sequences obtained suggest that the E. coli and B. stearothermophilus proteins have retained structural homology in this region, whereas the H. cutirubrum proteins have not.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002918:Chymotrypsin; D004926:Escherichia coli / Q000032:analysis*; D001411:Geobacillus stearothermophilus / Q000032:analysis*; D006217:Halobacterium / Q000032:analysis*; D010454:Peptide Termination Factors / Q000032:analysis; D012269:Ribosomal Proteins / Q000032:analysis*; D013045:Species Specificity; D013820:Thermolysin
D000596:Amino Acids; D010454:Peptide Termination Factors; D012269:Ribosomal Proteins; D002918:Chymotrypsin; D013820:Thermolysin