TY - JOUR TI - Novel RNA and DNA strand exchange activity of the PALB2 DNA binding domain and its critical role for DNA repair in cells AU - Deveryshetty, Jaigeeth AU - Peterlini, Thibaut AU - Ryzhikov, Mikhail AU - Brahiti, Nadine AU - Dellaire, Graham AU - Masson, Jean-Yves AU - Korolev, Sergey A2 - Spies, Maria A2 - Wolberger, Cynthia A2 - Spies, Maria A2 - Dillingham, Mark Simon VL - 8 PY - 2019 DA - 2019/04/24 SP - e44063 C1 - eLife 2019;8:e44063 DO - 10.7554/eLife.44063 UR - https://doi.org/10.7554/eLife.44063 AB - BReast Cancer Associated proteins 1 and 2 (BRCA1, −2) and Partner and Localizer of BRCA2 (PALB2) protein are tumour suppressors linked to a spectrum of malignancies, including breast cancer and Fanconi anemia. PALB2 coordinates functions of BRCA1 and BRCA2 during homology-directed repair (HDR) and interacts with several chromatin proteins. In addition to protein scaffold function, PALB2 binds DNA. The functional role of this interaction is poorly understood. We identified a major DNA-binding site of PALB2, mutations in which reduce RAD51 foci formation and the overall HDR efficiency in cells by 50%. PALB2 N-terminal DNA-binding domain (N-DBD) stimulates the function of RAD51 recombinase. Surprisingly, it possesses the strand exchange activity without RAD51. Moreover, N-DBD stimulates the inverse strand exchange and can use DNA and RNA substrates. Our data reveal a versatile DNA interaction property of PALB2 and demonstrate a critical role of PALB2 DNA binding for chromosome repair in cells. KW - DNA recombination KW - DNA repair KW - protein-DNA interaction KW - tumor supressor JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -