
@article {115813,
	title = {Double DJ-1 domain containing Arabidopsis DJ-1D is a robust macromolecule deglycase.},
	journal = {New Phytol},
	year = {2022},
	month = {2022 Jul 31},
	abstract = {<p>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.</p>
},
	issn = {1469-8137},
	doi = {10.1111/nph.18414},
	author = {Prasad, Melvin and Kataria, Priyanka and Ningaraju, Sunayana and Buddidathi, Radhika and Bankapalli, Kondalarao and Swetha, Chenna and Susarla, Gautam and Venkatesan, Radhika and D{\textquoteright}Silva, Patrick and Shivaprasad, Padubidri V}
}
