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Evolution of bacterial ribosomal protein L1
William L Duax1, Robert Huether, David Dziak
1Department of Structural Biology, Hauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA. duax@hwi.buffalo.edu
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.
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