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The chromatin fiber is a complex of DNA and specific proteins called histonesforming the first structural level of organization of eukaryotic chromosomes.In tightly organized chromatin fibers, the short segments of naked DNA linkingthe nucleosomes are strongly end constrained. Longitudinal thermal fluctuationsin these linkers allow intercalative mode of protein binding. We show thatmechanical constraints generated in the first stage of the binding processinduce linker DNA buckling; buckling in turn modifies the binding energies andactivation barriers and creates a force of decondensation at the chromatinfiber level. The unique structure and properties of DNA thus yield a novelphysical mechanism of buckling instability that might play a key role in theregulation of gene expression.Comment: 5 pages, 4 figures. To appear in Physical Review E (Rapid  Communication

Intercalation and buckling instability of DNA linker within locked chromatin fiber