The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation

Andrew Bowman, Richard Ward, Nicola Wiechens, Vijender Singh, Hassane El Mkami, David George Norman, Tom Owen-Hughes*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)

Abstract

Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.

Original languageEnglish
Pages (from-to)398-408
Number of pages11
JournalMolecular Cell
Volume41
Issue number4
DOIs
Publication statusPublished - 18 Feb 2011

Keywords

  • NUCLEOSOME ASSEMBLY PROTEIN-1
  • DNA-REPLICATION
  • ACETYLTRANSFERASE RTT109
  • CRYSTAL-STRUCTURE
  • STRUCTURAL BASIS
  • COMPLEXES
  • CORE
  • CHROMATIN
  • ACETYLATION
  • ASF1

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