Аннотация:Polymorphisms of 62 peroxidase genes derived from Arabidopsis thaliana
were investigated to evaluate evolutionary dynamics and divergence of peroxidase
proteins. By comparing divergence of duplicated genes AtPrx53-AtPrx54 and AtPrx36-
AtPrx72 and their products, nucleotide and amino acid substitutions were identified that
were apparently targets of positive selection. These substitutions were detected among
paralogs of 461 ecotypes from Arabidopsis thaliana. Some of these substitutions are
conservative and matched paralogous peroxidases in other Brassicaceae species. These
results suggest that after duplication, peroxidase genes evolved under positive selection,
and amino acid substitutions identified during our study provided divergence of
properties and physiological functions in peroxidases. Our predictions regarding
functional significance for amino acid residues identified in variable sites of peroxidases
may allow further experimental assessment of evolution of peroxidases after gene
duplication.