A retroelement-derived mammalian Arc protein exhibits selective RNA recognition and nucleic acid chaperone functions

This dataset contains raw and processed data supporting the study of the interaction between rat ARC protein and RNA, and ARC’s nucleic acid chaperone (NAC) activity. The data were collected using several complementary approaches: Microscale Thermophoresis (MST):Binding affinities between the protein and various RNA molecules were measured using MST (NanoTemper Monolith). The dataset includes raw MST traces, processed data, and calculated EC₅₀ values. NAC activity assays:The dataset includes quantification of gel images from assays testing the NAC activity of ARC (Strand displacement assay, TAR annealing assay, Ty3 RNA dimerization and tRNAiMet annealing assays). The dataset includes CSV tables with normalized band intensities. RNA 3D structure modeling:Predicted tertiary structures of the studied RNA molecules were generated using RNAComposer. The dataset includes input files (.txt) with the RNA secondary structure and PDB files of RNA models. Protein–RNA complex docking:Structural models of protein–RNA complexes were obtained using docking simulations with HADDOCK 2.4. The dataset includes input files, docked complex structures (PDB format), and scoring results. All experimental conditions, file types, and analysis methods are documented in the included README.txt file. Keywords:ARC, protein–RNA interaction, microscale thermophoresis, RNA chaperone, gel quantification, RNA 3D structure, docking.