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ADP-ribosyltransferases (ARTs) modify proteins with single units or polymers of ADP-ribose to regulate DNA repair. However, the substrates for these enzymes are ill-defined. For example, although histones are modified by ARTs, the sites on these proteins ADP-ribosylated following DNA damage and the ARTs that catalyse these events are unknown. This, in part, is due to the lack of a eukaryotic model that contains ARTs, in addition to histone genes that can be manipulated to assess ADP-ribosylation events  in vivo . Here we exploit the model  Dictyostelium  to identify site-specific histone ADP-ribosylation events  in vivo  and define the ARTs that mediate these modifications.  Dictyostelium  histones are modified in response to DNA double strand breaks (DSBs)  in vivo  by the ARTs Adprt1a and Adprt2. Adprt1a is a mono-ART that modifies H2BE18  in vitro , although disruption of this site allows ADP-ribosylation at H2BE19. Although redundancy between H2BE18 and H2BE19 ADP-ribosylation is also apparent following DSBs  in vivo , by generating a strain with mutations at E18/E19 in the  h2b  locus we demonstrate these are the principal sites modified by Adprt1a/Adprt2. This identifies DNA damage induced histone mono-ADP-ribosylation sites by specific ARTs  in vivo , providing a unique platform to assess how histone ADP-ribosylation regulates DNA repair.

Site-specific ADP-ribosylation of histone H2B in response to DNA double strand breaks