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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)
1 Downloads (Pure)


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
Pages (from-to)6038-6051
Number of pages14
JournalNucleic Acids Research
Issue number9
Early online date31 Mar 2014
Publication statusPublished - 2014


  • Nucleosome assembly protein-1
  • Angle scattering data
  • X-ray-scattering
  • Acetyltransferase Rtt109
  • Saccharomyces-cerevisiae
  • Transcription elongation
  • In-vitro
  • Complexes
  • Acetylation
  • Association


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