Prasad, M and Kataria, P and Ningaraju, S and Buddidathi, R and Bankapalli, K and Swetha, C and Susarla, G and Venkatesan, R and D'Silva, P and Shivaprasad, PV (2022) Double DJ-1 domain containing Arabidopsis DJ-1D is a robust macromolecule deglycase. In: New Phytologist .
Full text not available from this repository.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. © 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.
| Item Type: | Journal Article |
|---|---|
| Publication: | New Phytologist |
| Publisher: | John Wiley and Sons Inc |
| Additional Information: | The copyright for this article belongs to Wiley. |
| Department/Centre: | Division of Biological Sciences > Biochemistry |
| Date Deposited: | 06 Sep 2022 07:15 |
| Last Modified: | 06 Sep 2022 07:15 |
| URI: | https://eprints.iisc.ac.in/id/eprint/76486 |
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