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

Shuchismita Dutta, Ildikó V. Akey, Colin Dingwall, Kari L. Hartman, Tom Laue, Robert T. Nolte, James F. Head, Christopher W. Akey

Research output: Contribution to journalArticlepeer-review

134 Scopus citations

Abstract

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 Å resolution. The Np-core monomer is an eight-stranded β 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.

Original languageEnglish (US)
Pages (from-to)841-853
Number of pages13
JournalMolecular cell
Volume8
Issue number4
DOIs
StatePublished - 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly'. Together they form a unique fingerprint.

Cite this