Fernández-Rivero…Prado {Sci Rep 6: 32114}

A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility. Sci Rep. 2016 Aug 25;6:32114. doi: 10.1038/srep32114.
A. Nucleoplasmin (NP) binds core histones with high affinity forming complexes that differ in the stoichiometry and architecture. Binding models, based on EM data, for the interaction of NP with H2A-H2B (red) and H3-H4 (green). B. The affinity of NP for nucleosomal and linker histones is modulated by phosphorylation and intramolecular interactions that regulate the accessibility of the acidic tract at the intrinsically disordered distal face of the chaperone. Kd values for the interaction of phosphorylated (egg NP and oocyte NP) and non-phosphorylated (recombinant, full-length –rNP- or deletion mutants that lack the entire -rNPΔ120-200- or part - rNPΔ150-200- of the tail domain) NPs with histones.