title: Examination of protein sequence homologies. VI. The evolution of Escherichia coli L7/L12 equivalent ribosomal proteins ('A' proteins), and the tertiary structure.
abstract: Sequence homologies among 23 complete and two partial sequences of ribosomal 'A' proteins from eukaryotes, metabacteria, eubacteria and chloroplasts, equivalent to Escherichia coli L7/L12, were examined using a correlation method that evaluates sequence similarity quantitatively. Examination of 325 comparison matrices prepared for possible combinations of the sequences indicates that 'A' protein sequences can be classified into two types: one is the "prototype" from eubacteria and chloroplasts, and the other is the "transposition type" from eukaryotes and metabacteria, which must have resulted from the internal transposition of the prototype sequence. The transposition type of eukaryotes can further be classified into P1 and P2 lines. Sequences of the P1 line are closer to those of metabacteria than to those of the P2 line. Eleven gaps, as deletion or insertion sites of amino acid residues, are necessary for an alignment of all the sequences. According to the crystallographic data for the C-terminal fragment (CTF) from E. coli L7, all the gaps involved in the CTF are located between segments that correspond to structural and functional elements such as alpha helix, beta strand, turning loop or hinge part. The existence of specific "preservation units" in these molecules is suggested. In contrast, the transposition site is located at the center of an alpha helix element that is involved in a folding domain, indicating that the transposition event was extremely drastic.
authors.affiliation: Department of Biochemistry and Biophysics, Hiroshima University, Japan.
authors.forename: E
authors.initials: E
authors.lastname: Otaka
authors.forename: T
authors.initials: T
authors.lastname: Ooi
authors.forename: K
authors.initials: K
authors.lastname: Suzuki
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000032:analysis; D005075:Biological Evolution; D003198:Computer Simulation; D004330:Drosophila / Q000032:analysis; D004926:Escherichia coli / Q000032:analysis*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012269:Ribosomal Proteins; D012440:Saccharomyces / Q000032:analysis; D012689:Sequence Homology, Nucleic Acid
chemical_list: D012269:Ribosomal Proteins