Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses

Cécilia Hognon; Tom Miclot; Cristina Garcia Iriepa; Antonio Francés-Monerris; Stephanie Grandemange; Alessio Terenzi; Marco Marazzi; Giampaolo Barone; Antonio Monari

. CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.07.029447 doi: bioRxiv preprint The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.07.029447 doi: bioRxiv preprint 13 interactions and appears to be more stable and is essential in rigidifying the protein dimer and stabilizing the SUD-G4 interface, the latter assures a great flexibility to the protein and is guided by dispersion interactions. Such stable interaction between SUD and G4-RNA can be related to the translational default of the concerned proteins (see Figure 1) . Furthermore, the monomer interaction mode, happening in a more solvent exposed region of the protein, can also play a role in recruiting RNA fragments in the first step of the SUD-G4 recognition.