DNA end resection is required for accurate processing of broken DNA. In a paper published in Nature Communications, IRB researchers Acharya, Cejka and colleagues investigated the interplay of the Dna2 nuclease and the single strand DNA binding protein RPA in DNA end resection. RPA has a strong affinity to ssDNA, and often acts in DNA metabolism non-specifically to protect unwound DNA. In the resection process however, RPA plays a much more direct role, in fact, it stimulates Dna2 recruitment and its helicase and nuclease activities, which are important for DNA end resection. The authors define the various RPA domains involved in Dna2 regulation, and find that distinct RPA domains are involved in the regulation of the different Dna2 functions. The research stems from a collaboration between researchers from IRB Bellinzona, ETH Zurich, University of Leipzig (Germany) and CNRS (France).
Distinct RPA domains promote recruitment and the helicase-nuclease activities of Dna2
Ananya Acharya, Kristina Kasaciunaite, Martin Göse, Vera Kissling, Raphaël Guérois, Ralf Seidel & Petr Cejka
Nature Communications (2021), 12: 6521