Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A

Naoki Horikoshi, Yasuhiro Arimura, Hiroyuki Taguchi, Hitoshi Kurumizaka*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.

Original languageEnglish
Article number160127
JournalOpen Biology
Issue number6
Publication statusPublished - 2016 Jun 1


  • Chromatin
  • Crystal structure
  • H2A.Z
  • H2a.z l1 loop
  • Heterotypic nucleosome
  • Nucleosome

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • General Neuroscience
  • Immunology


Dive into the research topics of 'Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A'. Together they form a unique fingerprint.

Cite this