Structural and Biochemical Characterization of Poly-ADP-ribose Polymerase from Trypanosoma brucei.

ABSTRACT: 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. T. brucei PARP, like human PARPs-1-3, is activated by DNA binding and it potentially functions in DNA repair processes. Here we characterized activation requirements, structure and subcellular localization of T. brucei PARP. T. brucei PARP was found to be selectively activated by 5' phosphorylated and 3' phosphorylated DNA breaks. Importantly, the N-terminal region is responsible for high-affinity DNA-binding and required for DNA-dependent enzymatic activation. This modul

SUBMITTER: Haikarainen T 

PROVIDER: S-EPMC5473844 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature