Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans

Nat Commun. 2019 Apr 2;10(1):1491. doi: 10.1038/s41467-019-09153-6.


Poly-ADP-ribosylation, a post-translational modification involved in various cellular processes, is well characterized in eukaryotes but thought to be devoid in bacteria. Here, we solve crystal structures of ADP-ribose-bound poly(ADP-ribose)glycohydrolase from the radioresistant bacterium Deinococcus radiodurans (DrPARG), revealing a solvent-accessible 2'-hydroxy group of ADP-ribose, which suggests that DrPARG may possess endo-glycohydrolase activity toward poly-ADP-ribose (PAR). We confirm the existence of PAR in D. radiodurans and show that disruption of DrPARG expression causes accumulation of endogenous PAR and compromises recovery from UV radiation damage. Moreover, endogenous PAR levels in D. radiodurans are elevated after UV irradiation, indicating that PARylation may be involved in resistance to genotoxic stresses. These findings provide structural insights into a bacterial-type PARG and suggest the existence of a prokaryotic PARylation machinery that may be involved in stress responses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / chemistry
  • Adenosine Diphosphate Ribose / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Biocatalysis
  • Deinococcus / enzymology*
  • Deinococcus / genetics
  • Deinococcus / metabolism
  • Deinococcus / radiation effects
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • Poly ADP Ribosylation / radiation effects
  • Poly Adenosine Diphosphate Ribose / chemistry
  • Poly Adenosine Diphosphate Ribose / metabolism
  • Substrate Specificity
  • Ultraviolet Rays


  • Bacterial Proteins
  • Adenosine Diphosphate Ribose
  • Poly Adenosine Diphosphate Ribose
  • Glycoside Hydrolases
  • poly ADP-ribose glycohydrolase