title: The conservation of amino acids in the n-terminal position of ribosomal and cytosol proteins from Escherichia coli, Bacillus stearothermophilus, and Halobacterium cutirubrum.
abstract: Alanine, methionine, and serine are the predominant N-terminal residues in the cytosol and ribosomal protein fractions from the thermophile Bacillus stear othermophilus and the extreme halophile Halobacterium cutirubrum, a similar situation to that previously found in Escherichia coli. In all three bacteria the N-terminal residues of the 30S ribosomal proteins are mainly alanine greater than methionine greater than serine whereas in the 50S ribosomal proteins from E. coli and B. stearothermophilus the predominant residues are methionine greater than alanine greater than serine suggesting conservation of specific N-terminal residues in these ribosomal proteins. However, the 50S ribosomal proteins from H. cutirubrum showed serine as the major N-terminal residue.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D006217:Halobacterium / Q000378:metabolism*; D006358:Hot Temperature; D012269:Ribosomal Proteins / Q000378:metabolism*; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D012269:Ribosomal Proteins