UBR7 acts as a histone chaperone for post-nucleosomal histone H3

EMBO J. 2021 Dec 15;40(24):e108307. doi: 10.15252/embj.2021108307. Epub 2021 Nov 17.


Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

Keywords: NASP; UBR7; chaperone; chromatin; histone.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autoantigens / metabolism*
  • Cell Line
  • HEK293 Cells
  • HeLa Cells
  • Histone Code
  • Histones / chemistry
  • Histones / metabolism*
  • Humans
  • Nuclear Proteins / metabolism*
  • Nucleosomes / metabolism
  • Protein Domains
  • Ubiquitin-Protein Ligases / metabolism*


  • Autoantigens
  • Histones
  • NASP protein, human
  • Nuclear Proteins
  • Nucleosomes
  • UBR7 protein, human
  • Ubiquitin-Protein Ligases