MITOCHONDRIAL AND NUCLEAR ENDONUCLEASE WEN1 AND WEN2 FROM WHEAT TRITICUM AESTIVUM L. AND MODULATION BY SHORT PEPTIDES OF THEIR ENZYME ACTIVITY

Original title

МИТОХОНДРИАЛЬНАЯ И ЯДЕРНАЯ ЭНДОНУКЛЕАЗЫ WEN1 И WEN2 ИЗ ПШЕНИЦЫ Triticumaestivum L. И МОДУЛЯЦИЯ КОРОТКИМИ ПЕПТИДАМИ ИХ ФЕРМЕНТАТИВНОЙ АКТИВНОСТИ

Authors

L.I. Fedoreyeva^1,2, B.F. Vanyushin^1,2

Contact information

¹All-Russia Research Institute of Agricultural Biotechnology RAS, Moscow, Russia

²A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia

Pages

145-146

DOI

10.31255/978-5-94797-318-1-145-146

Abstract

From the vesicular fraction of the aging coleoptile wheat Triticum aestivum L. two Ca2 +, Mg2 + -dependent WEN1 and WEN2 were isolated. The endonucleases WEN1 and WEN2 are sensitive to the status of DNA methylation. Endonuclease WEN2 preferably cleaves unmethylated, and WEN1 methylated DNA. S-adenosyl-L-methionine (SAM) significantly enhances the action of WEN2 endonuclease and inhibits WEN1. Adenine DNA-methyltransferase (WAD) was also isolated from aging coleoptiles of wheat seedlings. This is the first adenine DNA methyltransferase found in eukaryotes. The presence in the vesicular fraction of two endonucleases WEN1 and WEN2, sensitive to the status of DNA methylation, and whose activity can be regulated by SAM, and the presence of adenine DNA methyltransferase in the same fraction, is most likely due to the existence of epigenetic control (DNA methylation) behind nuclease activity in plants.

It is assumed that the endonucleases WEN1 and WEN2 and WAD-methylase can be molecular markers of programmed cell death in plants during aging, as well as under the influence of various abiotic stresses.

Short exogenous peptides inhibit or, on the contrary, stimulate the hydrolysis of DNA by the eukaryotic CNG and CG site with specific wheat endonucleases WEN1 and WEN2, depending on the status of DNA methylation. Modulation of enzyme activity by peptides can be due to the fact that peptides bind to certain DNA sites, as a result of which enzymes either compete with peptides for these sites, or the associated peptides facilitate the hydrolysis of DNA by enzymes.

It is assumed that site-specific interactions of peptides with DNA can epigenetically control the genetic functions of the cell.