Faculty of Biology, University of Latvia
EEB
Hard copy: ISSN 1691–8088
On-line: ISSN 2255–9582
Acta Univ Latv (2004) 676: 97–105
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Environmental and
Experimental
Biology

Acta Univ Latv (2004) 676: 97–105

Orginal Article

Origin of globins and a mystery of myoglobin codon root symmetry

Nora Ieviņa*, Gunārs Chipens
Department of Peptide Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Rīga LV-1006, Latvia
*Corresponding author, E-mail: ievina@osi.lv

Abstract

The amino acid sequence 49–94 of myoglobin involved in heam binding has 74 % symmetric codon roots – the second codon letters. The search for the reason of the symmetry revealed that the ancestor of globin genes was not formed by exon shuffling, but by multiplication of a 21-membered nucleotide and that it was a regular polynucleotide. The repeat unit pile of contemporary myoglobin codon root sequence posesses an inversion centre indicating that symmetry of codon roots evolved after the origin of globin gene. Its cause and possible biological functions is a mystery. A model of coding of the globin ancestor gene is suggested to be formed of identical repeat units separated by 23 introns.

Key words: multiplication of nucleotides, old ancestral introns, origin of introns, repeat units of genes and proteins.

 
Acta Univ Latv (2004) 676: 97–105
 DOI: http://doi.org/10.22364/eeb
EEB

Editor-in-Chief
Prof. Gederts Ievinsh



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University of Latvia

 
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