The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly

Mol Cell. 2001 Oct;8(4):841-53. doi: 10.1016/s1097-2765(01)00354-9.


The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Histones / chemistry
  • Histones / metabolism*
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Nucleoplasmins
  • Nucleosomes / metabolism*
  • Phosphoproteins / chemistry*
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary*
  • Sequence Alignment


  • Histones
  • Macromolecular Substances
  • Nuclear Proteins
  • Nucleoplasmins
  • Nucleosomes
  • Phosphoproteins