Dynamical DNA accessibility induced by chromatin remodeling and protein binding

F Montel 1 Cendrine Faivre-Moskalenko 2 Martin Castelnovo 2, *
* Auteur correspondant
1 MSC - Laboratoire Matière et Systèmes Complexes
2 Phys-ENS - Laboratoire de Physique de l'ENS Lyon
Abstract : Chromatin remodeling factors are enzymes being able to alter locally chromatin structure at the nucleosomal level and they actively participate in the regulation of gene expression. Using simple rules for individual nucleosome motion induced by a remodeling factor, we designed simulations of the remodeling of oligomeric chromatin, in order to address quantitatively collective effects in DNA accessibility upon nucleosome mobilization. Our results suggest that accessibility profiles are inhomogeneous thanks to borders effects like protein binding. Remarkably, we show that the accessibility lifetime of DNA sequence is roughly doubled in the vicinity of borders as compared to its value in bulk regions far from the borders. These results are quantitatively interpreted as resulting from the confined diffusion of a large nucleosome depleted region.
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Physical Review E : Statistical, Nonlinear, and Soft Matter Physics, American Physical Society, 2014, 90, pp.052717. 〈10.1103/PhysRevE.90.052717〉
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ENS-LYON | UNIV-PARIS7 | USPC | UNIV-LYON1

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F Montel, Cendrine Faivre-Moskalenko, Martin Castelnovo. Dynamical DNA accessibility induced by chromatin remodeling and protein binding. Physical Review E : Statistical, Nonlinear, and Soft Matter Physics, American Physical Society, 2014, 90, pp.052717. 〈10.1103/PhysRevE.90.052717〉. 〈ensl-01084485〉

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