Xenopus laevis peroxiredoxins: Gene expression during development and characterization of the enzymes

• Published in: Molecular biology (New York) Vol. 50; no. 2; pp. 292 - 301
• Main Authors: Sharapov, M. G., Novoselov, V. I., Ravin, V. K.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.03.2016; Springer Nature B.V
• Subjects: Biochemistry; Biomedical and Life Sciences; Embryos; Enzymes; Escherichia coli; Gene expression; Homeostasis; Human Genetics; Life Sciences; Molecular biology; Molecular Cell Biology; Xenopus laevis; gene expression, vembryonic development; peroxiredoxins; reactive oxygen species
• ISSN: 0026-8933; 1608-3245
• DOI: 10.1134/S0026893316020217

Reactive oxygen species (ROS) are produced via catabolic and anabolic processes during normal embryonic development, and ROS content in the cell is maintained at a certain level. Peroxiredoxins are a family of selenium-independent peroxidases and play a key role in maintaining redox homeostasis of the cell. In addition to regulating the ROS level, peroxiredoxins are involved in intracellular and intercellular signaling, cell differentiation, and tissue development. The time course of peroxiredoxin gene ( prx1–6 ) expression was studied in Xenopus laevis during early ontogeny (Nieuwkoop and Faber stages 10–63). The highest expression level was observed for prx1 at these developmental stages. The prx1 , prx3 , and prx4 expression level changed most dramatically in response to oxidative stress artificially induced in X. laevis embryos. In X. laevis adults, prx1–6 were all intensely expressed in all organs examined, the prx1 expression level being the highest. The X. laevis prx1–6 genes were cloned and expressed in Escherichia coli , and physico-chemical characteristics were compared for the recombinant enzymes. The highest peroxidase activity and thermal stability were observed for Prx1 and Prx2. It was assumed that Prx1 plays a leading role in X. laevis early development.