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- Title
Double DJ‐1 domain containing Arabidopsis DJ‐1D is a robust macromolecule deglycase.
- Authors
Prasad, Melvin; Kataria, Priyanka; Ningaraju, Sunayana; Buddidathi, Radhika; Bankapalli, Kondalarao; Swetha, Chenna; Susarla, Gautam; Venkatesan, Radhika; D'Silva, Patrick; Shivaprasad, Padubidri V.
- Abstract
Summary: 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.
- Subjects
MACROMOLECULES; ARABIDOPSIS; DNA repair; NUCLEIC acids; NUCLEOTIDES
- Publication
New Phytologist, 2022, Vol 236, Issue 3, p1061
- ISSN
0028-646X
- Publication type
Article
- DOI
10.1111/nph.18414