The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

Research output: Contribution to journalJournal articleResearchpeer-review

  • Andrew Bowman
  • Hammond, Colin
  • Andrew Stirling
  • Richard Ward
  • Weifeng Shang
  • Hassane El Mkami
  • David A. Robinson
  • Dmitri I. Svergun
  • David G Norman
  • Tom Owen-Hughes

NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.

Original languageEnglish
JournalNucleic Acids Research
Issue number9
Pages (from-to)6038-51
Number of pages14
Publication statusPublished - May 2014
Externally publishedYes

    Research areas

  • Models, Molecular, Molecular Chaperones, Nucleosome Assembly Protein 1, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Scattering, Small Angle, Solutions, X-Ray Diffraction, Journal Article, Research Support, Non-U.S. Gov't

ID: 178883218