Kap114 and Nap1 ₂ co-chaperone H2A-H2B in the presence of Ran ^GTP . (A) Depicted as in Fig. 4 A, histone interaction interfaces in Nap1₂•H2A-H2B•Kap114•Ran^GTP and Ran^GTP•Kap114•H2A-H2B (8F1E). The green asterisks (*) indicate transient Ran^GTP-H2A-H2B contacts. H2B α1 (black oval) is likely inaccessible due to the proximity of Nap1₂ in Nap1₂•H2A-H2B•Kap114•Ran^GTP just like Nap1₂•H2A-H2B•Kap114; however, it is exposed in Ran^GTP•Kap114•H2A-H2B, likely explaining why histone is not effectively chaperoned in this complex. (B) DNA competition assays of DNA•H2A-H2B complex (D•H; 1 µM:4 µM) added to Kap114 (K) or Kap114+Nap1₂ mixture (K+N₂), with a titration of Ran^GTP (concentrations indicated in the table of summary of results below. Samples were visualized using ethidium bromide- and Coomassie-stained native PAGE gels. (C) Similar assay as in B, but all proteins were assembled in complexes before the addition of DNA. Source data are available for this figure: SourceData F5.