Skip to content
DraconiticResearch
Search Sources API
203,203 studies31 sourcesUpdated 1 h ago
PreprintCC BY-NCbioRxiv

INO80 rapidly shuttles nucleosomes between chromatin barriers

  1. 1Imperial College London

Abstract

ATP-dependent chromatin remodelers establish nucleosome organization, but how they move nucleosomes over extended distances and respond to neighboring chromatin remains unclear. Here, we combine correlative optical tweezers and fluorescence microscopy, and single-molecule FRET to visualize human INO80 activity on naked and chromatinized DNA. hINO80 undergoes free one-dimensional diffusion along DNA with multiple, nucleotide-regulated, diffusive states. Upon engaging a nucleosome, hINO80 drives rapid, processive nucleosome sliding over thousands of base pairs in bidirectional bursts. Neighboring nucleosomes prevent passage and redirect translocation, confining mobile nucleosomes to repeated movement between chromatin boundaries. Single-molecule FRET reveals transitions consistent with INO80 switching between opposing nucleosome-binding orientations, while fluorescence stoichiometry and mass photometry show that two hINO80 complexes can simultaneously occupy one nucleosome. These findings identify non-exclusive mechanisms for directional reversal and reveal how long-range hINO80 translocation is converted into boundary-constrained nucleosome repositioning, providing a dynamic framework for understanding nucleosome organization within chromatin.

Related

  1. Three-dimensional chromatin architecture is rapidly restored after DNA replication.
    Tyler K Fenstermaker, Svetlana Petruk, Alexander Mazo
    Nature communicationsPeer-reviewedCC BY-NC-NDFull textMolecular biology & gene regulationEurope PMC
  2. Mechanisms of INO80 remodeling
    Shagun Shukla, Blaine Bartholomew
    Biochemical Society TransactionsPeer-reviewedCC BY 4.0Full textEnzymology & metabolismPMC
  3. Sequence-dependent binding modes of INO80 control +1 nucleosome positioning
    M. Likhodeeva, A. Brem, A. Lopez-Francos +9
    bioRxivPreprintCC BY-NC-NDFull textMolecular biology & gene regulationbioRxiv
  4. CRISPR-mediated gap-based replacement enables site-specific DNA lesion insertion into long DNA and nucleosomes
    Nucleic acids researchPeer-reviewedCC BYFull textMolecular biology & gene regulationEurope PMC
  5. Histone modifications directly modulate transcription factor binding to nucleosomes
    Luca Mariani, Martha L. Bulyk
    bioRxivPreprintCC BY-NC-NDFull textMolecular biology & gene regulationbioRxivEurope PMCPMC
BibTeX
@misc{ambrose2026ino80,
  title = {{INO80 rapidly shuttles nucleosomes between chromatin barriers}},
  author = {B. Ambrose and P. Girvan and M. T. Skehan and E. A. McCormack and D. I. Egharevba and D. S. Rueda},
  howpublished = {bioRxiv},
  year = {2026},
  month = sep,
  doi = {10.64898/2026.09.20.752975},
  url = {https://www.biorxiv.org/content/10.64898/2026.09.20.752975v1},
  note = {CC BY-NC},
}
RIS
TY  - UNPB
TI  - INO80 rapidly shuttles nucleosomes between chromatin barriers
AU  - B. Ambrose
AU  - P. Girvan
AU  - M. T. Skehan
AU  - E. A. McCormack
AU  - D. I. Egharevba
AU  - D. S. Rueda
PY  - 2026
DA  - 2026/09/20
PB  - bioRxiv
DO  - 10.64898/2026.09.20.752975
UR  - https://www.biorxiv.org/content/10.64898/2026.09.20.752975v1
AB  - ATP-dependent chromatin remodelers establish nucleosome organization, but how they move nucleosomes over extended distances and respond to neighboring chromatin remains unclear. Here, we combine correlative optical tweezers and fluorescence microscopy, and single-molecule FRET to visualize human INO80 activity on naked and chromatinized DNA. hINO80 undergoes free one-dimensional diffusion along DNA with multiple, nucleotide-regulated, diffusive states. Upon engaging a nucleosome, hINO80 drives rapid, processive nucleosome sliding over thousands of base pairs in bidirectional bursts. Neighboring nucleosomes prevent passage and redirect translocation, confining mobile nucleosomes to repeated movement between chromatin boundaries. Single-molecule FRET reveals transitions consistent with INO80 switching between opposing nucleosome-binding orientations, while fluorescence stoichiometry and mass photometry show that two hINO80 complexes can simultaneously occupy one nucleosome. These findings identify non-exclusive mechanisms for directional reversal and reveal how long-range hINO80 translocation is converted into boundary-constrained nucleosome repositioning, providing a dynamic framework for understanding nucleosome organization within chromatin.
ER  -