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Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

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Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).

Tianjin Yang¹, Soundhararajan Gopi¹, Louise Pinet¹

¹Department of Biochemistry, University of Zurich, 8057 Zurich, Switzerland.

Biorxiv : the Preprint Server for Biology

|April 29, 2026

Summary

This summary is machine-generated.

Poly(ADP-ribose) (PAR) chains, crucial for DNA repair, compact and decompact nucleosomes. Longer PAR chains rapidly open nucleosomes, while shorter ones have minimal effect, revealing PAR length

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Poly(ADP-ribose) (PAR) synthesis is integral to cellular DNA damage response.
The precise impact of PAR on nucleosome structure and dynamics requires further elucidation.

Purpose of the Study:

To investigate the kinetics of PAR-induced nucleosome decompaction using advanced single-molecule techniques.
To determine the influence of PAR chain length and concentration on nucleosome remodeling.

Main Methods:

Utilized droplet-based microfluidics for rapid mixing and tether-free single-molecule Förster resonance energy transfer (smFRET) spectroscopy.
Performed non-equilibrium measurements with millisecond resolution to capture transient nucleosome dynamics.
Employed enzymatic PAR digestion and coarse-grained molecular simulations.

Main Results:

Identified a length-dependent kinetic threshold for PAR-induced nucleosome decompaction; longer PAR chains (>10 ADP-ribose units) trigger rapid opening.
Observed that decompaction extent and reversibility are modulated by PAR concentration and ionic strength, indicating electrostatic interactions are key.
Demonstrated that PAR can mediate both reversible linker DNA opening and irreversible nucleosome disassembly.
Molecular simulations suggest competition between PAR and histone tails for DNA binding.

Conclusions:

PAR chain length is a critical determinant of chromatin accessibility during DNA repair.
Electrostatic interactions and competition for histone tail binding govern PAR-nucleosome interactions.
Droplet-based microfluidics offers a powerful platform for studying biomolecular interactions with high temporal resolution.