Evolution of bacterial ribosomal protein L1. (26th March 2012)

• Record Type: Journal Article
• Authors: Duax, William L.; Huether, Robert; Dziak, David
• Is Part Of: International journal of bioinformatics research and applications. Volume 8:Number 1/2(2012)
• Page Start: 99
• Page End: 111
• Publication Date: 2012-03-26
• Subjects: molecular evolution -- ribosome -- ribosomal protein L1 -- accurate alignment -- GARP -- Gly, Ala, Arg and Pro -- genetic code evolution -- gram positive bacteria -- gram negative bacteria; Bioinformatics -- Periodicals; 570.285
• Languages: English
• ISSNs: 1744-5485

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.