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Bilayers of nucleosome core particles.

A Leforestier¹, J Dubochet, F Livolant

¹Laboratoire de Physique des Solides, Bât 510, Université Paris Sud, F-91405 Orsay Cedex, France.

Biophysical Journal

|September 22, 2001

Summary

Nucleosome core particle interactions drive chromatin condensation. Self-assembled nucleosomes form tubules, revealing stacking and bilayer structures crucial for understanding how DNA compacts within cells.

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Area of Science:

Molecular Biology
Biophysics
Structural Biology

Background:

Chromatin condensation and decondensation are vital cellular processes.
Interactions between nucleosome core particles are implicated in these processes.

Purpose of the Study:

To investigate nucleosome core particle interactions in the absence of linker DNA and proteins.
To elucidate the structural organization and forces governing nucleosome self-assembly.

Main Methods:

Self-assembly of isolated nucleosome core particles under controlled ionic conditions.
High-resolution imaging of cryosections of vitrified samples.

Main Results:

Observation of an original lamellar mesophase forming tubules.
Detailed visualization of nucleosome core particles stacking into columns and aligning into bilayers.
Identification of attractive face-to-face and lateral polar interactions between particles.

Conclusions:

Nucleosome core particle interactions, particularly attractive and lateral polar forces, are key to chromatin compaction.
These interactions occur under physiological conditions, highlighting their importance in vivo.
The discovered structural organization provides insights into the mechanisms of chromatin compaction.

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