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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-AM-04
Exploring the Cellular ADP-Ribosylome in Deinococcus radiodurans
(NTU)
oChun-Hua Hsu
oly-ADP-ribosylation (PARylation) is a well-known post-translational modification (PTM) in eukaryotes, but its existence in bacteria remained unclear. Our omics analysis identified drb0099 (DrPARG) from Deinococcus radiodurans as upregulated following UV-induced DNA damage, suggesting its involvement in prokaryotic ADP-ribosylation. Structural analysis of ADP-ribose-bound DrPARG revealed a solvent-accessible 2'-hydroxy group, indicative of endo-glycohydrolase activity in PAR metabolism. High-resolution mutant structures and immunoprecipitation of PARylated proteins confirmed this role. Disrupting DrPARG expression led to PAR accumulation and impaired UV damage recovery.
Our findings provided the first confirmation of bacterial PARylation (APR) in D. radiodurans (Nat. Commun., 2019). To explore its function, we developed a mass spectrometry-based approach, identifying 111 UV-induced PARylated proteins enriched in DNA repair, replication, metabolism, and detoxification. Key pathways included nucleotide excision repair (NER), mismatch repair (MMR), and double-strand break (DSB) repair. These results highlight bacterial PARylation as a regulatory mechanism in stress responses. Ongoing research aims to further investigate its chemical biology and proteomics, providing new insights into bacterial DNA repair and cellular resilience.