title: Evolution of bacterial ribosomal protein L1.
abstract: Search vectors composed of Gly, Ala, Arg, and Pro (GARP) residues retrieve 98% of each of the ribosomal proteins in prokaryotic species with no false hits. Different combinations of G, A, R and P and insertions differentiate each ribosomal protein from all others. Amino acids in two sequence positions separate Gram+ from Gram- bacteria. Specific residues separate proteins of cyanobacteria and chloroplasts from all other species. Structural information played an essential role in developing a GARP based technique to achieve perfect sequence alignment. It is possible to understand why GARP residues are 100% conserved in specific positions in families of proteins present in all species.
authors.affiliation: Department of Structural Biology, Hauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA. duax@hwi.buffalo.edu
authors.forename: William L
authors.initials: WL
authors.lastname: Duax
authors.forename: Robert
authors.initials: R
authors.lastname: Huether
authors.forename: David
authors.initials: D
authors.lastname: Dziak
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics*; D002736:Chloroplasts / Q000378:metabolism; D017124:Conserved Sequence; D000458:Cyanobacteria / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000235:genetics*; D016415:Sequence Alignment
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C028546:ribosomal protein L1