Histones H1 are proteins within the cell nucleus which are highly dynamic; they diffuse within the cell nucleus and interact with the chromatin structure (DNA and associated proteins) through a process of binding and unbinding. This kinetic process of association-dissociation, which regulates the chromatin organization and DNA accessibility, has been shown to be driven by either slow or rapid interactions. When trying to describe this dynamics with a mathematical model one realizes that there could be different binding pathways of histone H1 to the chromatin structure. In this work, we use different systems of reaction-diffusion equations and experimental data to describe and quantify these different pathways. We then perform a model comparison analysis for the purpose of determining the most feasible binding mechanism of histone H1 and provide new meaningful biophysical information on histone H1 dynamics.

Histone H1 dynamics; Histone H1 binding pathway; model comparison.