Extended and dynamic linker histone-DNA Interactions control chromatosome compaction

Sergei Rudnizky, Hadeel Khamis, Yuval Ginosar, Efrat Goren, Philippa Melamed, Ariel Kaplan

Research output: Contribution to journalArticlepeer-review


Chromatosomes play a fundamental role in chromatin regulation, but a detailed understanding of their structure is lacking, partially due to their complex dynamics. Using single-molecule DNA unzipping with optical tweezers, we reveal that linker histone interactions with DNA are remarkably extended, with the C-terminal domain binding both DNA linkers as far as approximately ±140 bp from the dyad. In addition to a symmetrical compaction of the nucleosome core governed by globular domain contacts at the dyad, the C-terminal domain compacts the nucleosome's entry and exit. These interactions are dynamic, exhibit rapid binding and dissociation, are sensitive to phosphorylation of a specific residue, and are crucial to determining the symmetry of the chromatosome's core. Extensive unzipping of the linker DNA, which mimics its invasion by motor proteins, shifts H1 into an asymmetric, off-dyad configuration and triggers nucleosome decompaction, highlighting the plasticity of the chromatosome structure and its potential regulatory role.

Original languageEnglish
Pages (from-to)3410-3421.e4
JournalMolecular Cell
Issue number16
StatePublished - 19 Aug 2021


  • DNA unzipping
  • chromatin
  • chromatosome
  • compaction
  • linker histone
  • nucleosome
  • optical tweezers
  • single-molecule biophysics

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Extended and dynamic linker histone-DNA Interactions control chromatosome compaction'. Together they form a unique fingerprint.

Cite this