By screening for Arabidopsis genes activated by ionising radiation (IR)-ind
uced DNA damage, we have isolated a cDNA hybridising with a 3.2-kb mRNA tha
t accumulates rapidly and strongly in irradiated cell suspensions or whole
plants. The cDNA codes for a 110-kDa protein that is highly homologous to t
he 116-kDa vertebrate poly(ADP-ribose) polymerase (PARP-1). It is recognise
d by a human anti-PARP-1 antibody, binds efficiently to DNA strand interrup
tions in vitro, and catalyses DNA damage-dependent (ADP-ribose) polymer syn
thesis. We have named this protein AtPARP-1. We have also extended our obse
rvations to the Arabidopsis app (AtPARP-2) gene, demonstrating for the firs
t time that IR-induced DNA strand interruptions induce rapid and massive ac
cumulation of AtPARP-1 and AtPARP-2 transcripts, whereas dehydration and ca
dmium preferentially induce the accumulation of AtPARP-2 transcripts. The I
R-induced PARP gene expression seen in Arabidopsis is in striking contrast
to the post-translational activation of the PARP-1 protein that is associat
ed with genotoxic stress in animal cells. AtPARP-1 transcripts accumulate i
n all plant organs after exposure to ionising radiation, but this is follow
ed by an increase in AtPARP-1 protein levels only in tissues that contain l
arge amounts of actively dividing cells. This cell-type specific accumulati
on of AtPARP-1 protein in response to DNA damage is compatible with a role
for the AtPARP-1 protein in the maintenance of DNA integrity during replica
tion, similar to the role of "guardian of the genome" attributed to its ani
mal counterpart.