Understanding Histone H1 Binding Mechanism Through Model Comparison and FRAP Experiments

Abstract

Histone H1 or linker histones play an important role in the package and order of DNA in eukaryotic cell nuclei by associating to and dissociating from the chromatin structure. Thus, in order to better understand the formation and stabilization of higher order chromatin structure it is crucial to understand the binding mechanism of histone H1. It has been hypothesized that histone H1 can bind in both a strong and a weak fashion to the chromatin structure. In this work, we use Flourescence Recovery After Photobleaching (FRAP) experiments together with model comparison criteria in order to support this hypothesis. We propose a feasible histone H1 binding mechanism, described with a system of reaction diffusion equations that is consistent with the experimental data and the existence of a weakly bound and a strongly bound population.