Evolutionary divergence of Arabidopsis thaliana classical peroxidases

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 substitution...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2015-10, Vol.80 (10), p.1362-1372
Main Authors: Kupriyanova, E. V., Mamoshina, P. O., Ezhova, T. A.
Format: Article
Language:English
Subjects:
Alleles
Amino Acid Sequence
Amino Acid Substitution
Amino acids
Arabidopsis - enzymology
Arabidopsis - genetics
Arabidopsis thaliana
Biochemistry
Biological diversity
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Cell growth
Ecotypes
Evolution, Molecular
Gene expression
Genetic aspects
Genetic polymorphisms
Hydrogen peroxide
Life Sciences
Microbiology
Molecular Sequence Data
Observations
Peroxidase
Peroxidases - chemistry
Peroxidases - genetics
Physiological aspects
Polymorphism
Polymorphism, Genetic
Proteins
Selection, Genetic
Sequence Homology, Nucleic Acid
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Summary: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 the pressure of 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.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297915100181