title: Electrostatic effect of H1-histone protein binding on nucleosome repeat length.
abstract: Within a simple biophysical model we describe the effect of electrostatic binding of H1 histone proteins on the nucleosome repeat length in chromatin. The length of wrapped DNA optimizes its binding energy to the histone core and the elastic energy penalty of DNA wrapping. The magnitude of the effect predicted from our model is in agreement with the systematic experimental data on the linear variation of nucleosome repeat lengths with H1/nucleosome ratio (Woodcock C L et al 2006 Chromos. Res. 14 17-25). We compare our model to the data for different cell types and organisms, with a widely varying ratio of bound H1 histones per nucleosome. We underline the importance of this non-specific histone-DNA charge-balance mechanism in regulating the positioning of nucleosomes and the degree of compaction of chromatin fibers in eukaryotic cells.
authors: Institute for Physics and Astronomy, University of Potsdam, 14476 Potsdam-Golm, Germany.
authors: Andrey G
authors: AG
authors: Cherstvy
authors: Vladimir B
authors: VB
authors: Teif
mesh_terms: D000818:Animals; D055592:Biophysical Phenomena; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding; D055672:Static Electricity
chemical_list: D006657:Histones; D009707:Nucleosomes