Double DJ-1 domain containing Arabidopsis DJ-1D is a robust macromolecule deglycase

New Phytol. 2022 Nov;236(3):1061-1074. doi: 10.1111/nph.18414. Epub 2022 Aug 17.

Abstract

Plants, being sessile, are prone to genotoxin-induced macromolecule damage. Among the inevitable damaging agents are reactive carbonyls that induce glycation of DNA, RNA and proteins to result in the build-up of advanced glycated end-products. However, it is unclear how plants repair glycated macromolecules. DJ-1/PARK7 members are a highly conserved family of moonlighting proteins having double domains in higher plants and single domains in other phyla. Here we show that Arabidopsis DJ-1D offers robust tolerance to endogenous and exogenous stresses through its ability to repair glycated DNA, RNA and proteins. DJ-1D also reduced the formation of reactive carbonyls through its efficient methylglyoxalase activity. Strikingly, full-length double domain-containing DJ-1D suppressed the formation of advanced glycated end-products in yeast and plants. DJ-1D also efficiently repaired glycated nucleic acids and nucleotides in vitro and mitochondrial DNA in vivo under stress, indicating the existence of a new DNA repair pathway in plants. We propose that multi-stress responding plant DJ-1 members, often present in multiple copies among plants, probably contributed to the adaptation to a variety of endogenous and exogenous stresses.

Keywords: Arabidopsis thaliana; DJ-1 family proteins; DNA repair; advanced glycation end-products; glycation; methylglyoxal; reactive carbonyls; stress responses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis* / genetics
  • DNA, Mitochondrial
  • Lactoylglutathione Lyase*
  • Mutagens
  • Nucleic Acids*
  • Nucleotides
  • RNA

Substances

  • DNA, Mitochondrial
  • Mutagens
  • Nucleic Acids
  • Nucleotides
  • RNA
  • Lactoylglutathione Lyase