Plasmodium falciparum, the main agent that causes malaria, is exposed to extensive DNA damage when it replicates in red blood cells. Remarkably, this parasite can very robustly repair DNA double-strand breaks despite the evolutionary loss of non-homologous end joining, the primary DNA repair pathway in eukaryotes. Here, Ron Dzikowski and colleagues (Goyal et al., 2021) address the molecular basis of this poorly understood adaptation. Applying a proteomic approach, they find that the splicing factor PfSR1 interacts with proteins involved in RNA metabolism as well as the DNA damage response. The authors then show that PfSR1 is indeed recruited to sites of DNA damage, where it is required for the accumulation of PfRad51, a factor that catalyses DNA repair. Using CRISPR-Cas9, they engineer a transgenic P. falciparum line to knock down PfSR1 in an inducible manner and demonstrate that the parasite needs PfSR1 to overcome DNA damage caused by either X-ray irradiation or the antimalarial drug artemisinin. Taken together, this work identifies PfSR1 as an important novel factor that protects P. falciparum from different sources of DNA damage and provides a new perspective for understanding the parasite's resistance to artemisinin.