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Primordia Vita. Deconvolution from Modern Sequences.
Authors:Edward N. Trifonov  Idan Gabdank  Danny Barash  Yehoshua Sobolevsky
Affiliation:(1) Genome Diversity Center, Institute of Evolution, University of Haifa, Haifa, 31905, Israel;(2) Department of Computer Science, Ben Gurion University of the Negev, P.O. Box 653, Be’er Sheva, 84105, Israel
Abstract:Evolution of the triplet code is reconstructed on the basis of consensus temporal order of appearance of amino acids. Several important predictions are confirmed by computational sequence analyses. The earliest amino acids, alanine and glycine, have been encoded by GCC and GGC codons, as today. They were succeeded, respectively, by A- and G-series of amino acids, encoded by pyrimidine-central and purine-central codons. The length of the earliest proteins is estimated to be 6–7 residues. The earliest mRNAs were short G+C-rich molecules. These short sequences could have formed hairpins. This is confirmed by analysis of modern prokaryotic mRNA sequences. Predominant size of detected ancient hairpins also corresponds to 6–7 amino acids, as above. Vestiges of last common ancestor can be found in extant proteins in form of entirely conserved short sequences of size six to nine residues present in all or almost all sequenced prokaryotic proteomes (omnipresent motifs). The functions of the topmost conserved octamers are not involved in the basic elementary syntheses. This suggests an initial abiotic supply of amino acids, bases and sugars. Presented at: National Workshop on Astrobiology: Search for Life in the Solar System, Capri, Italy, 26 to 28 October, 2005.
Keywords:abiotic synthesis  ancient binary alphabet of proteins  earliest mini-genes  earliest mRNA  earliest proteins  evolution of triplet code  last common ancestor  origin of life  reconstruction of ancient sequences
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