NDLI: Evolutionary divergence of Arabidopsis thaliana classical peroxidases

Content Provider	Springer Nature Link
Author	Kupriyava, E. V. Mamoshina, P. O. Ezhova, T. A.
Copyright Year	2015
Abstract	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.
Starting Page	1362
Ending Page	1372
Page Count	11
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	80
Issue Number	10
e-ISSN	16083040
Language	English
Publisher	Pleiades Publishing
Publisher Date	2015-10-17
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	peroxidase Arabidopsis thaliana gene and protein polymorphism gene duplication evolution divergence of protein properties bioinformatic analysis Biochemistry Bioorganic Chemistry Microbiology Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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