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Trypanosoma brucei is a unicellular parasite responsible for African trypanosomiasis or sleeping sickness.It contains a single PARP enzyme opposed to many higher eukaryotes, which have numerous PARPs.PARPs are responsible for a post-translational modification, ADP-ribosylation, regulating a multitude of cellular events. brucei PARP, like human PARPs-1-3, is activated by DNA binding and it potentially functions in DNA repair processes. brucei PARP was found to be selectively activated by 5′ phosphorylated and 3′ phosphorylated DNA breaks.Here we characterized activation requirements, structure and subcellular localization of T. Importantly, the N-terminal region is responsible for high-affinity DNA-binding and required for DNA-dependent enzymatic activation.

Comparison of Tb PARP domain structure to human PARPs-2-3 and a schematic presentation of the Tb PARP constructs used in the study.

In humans the family consists of 17 members, where PARPs are involved in a multitude of cellular processes including DNA damage repair, cell death pathways, and mitosis.

Human PARPs (h PARPs)-1-3, whose catalytic activity is induced by DNA-binding.

Interestingly, cytotoxicity induced by hydrogen peroxide was reduced both by down-regulation and inhibition of the catalytic activity of the enzyme suggesting a role for Tb PARP in cell death pathways.

In addition, inhibition of the catalytic activity of Tb PARP did not inhibit the growth of T. Here, in effort to understand the role of PARP in the parasite, we have characterized DNA-binding and DNA-dependent activation properties of the enzyme and especially the role of the N-terminal domain in these processes.

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