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In the early-diverging protozoan parasite  Plasmodium , few telomere-binding proteins have been identified and several are unique.  Plasmodium  telomeres, like those of most eukaryotes, contain guanine-rich repeats that can form G-quadruplex structures. In model systems, quadruplex-binding drugs can disrupt telomere maintenance and some quadruplex-binding drugs are potent anti-plasmodial agents. Therefore, telomere-interacting and quadruplex-interacting proteins may offer new targets for anti-malarial therapy. Here, we report that  P. falciparum  GBP2 is such a protein. It was identified  via  ‘Proteomics of Isolated Chromatin fragments’, applied here for the first time in  Plasmodium .  In vitro ,  Pf GBP2 binds specifically to G-rich telomere repeats in quadruplex form and it can also bind to G-rich RNA.  In vivo ,  Pf GBP2 partially colocalises with the known telomeric protein HP1 but is also found in the cytoplasm, probably due to its affinity for RNA. Consistently, its interactome includes numerous RNA-associated proteins.  Pf GBP2 is evidently a multifunctional DNA/RNA-binding factor in  Plasmodium .

Plasmodium falciparum GBP2 Is a Telomere-Associated Protein That Binds to G-Quadruplex DNA and RNA