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Electrostatic effect of H1-histone protein binding on nucleosome repeat length

  • 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.

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Metadaten
Author details:Andrey G. CherstvyORCiD, Vladimir B. Teif
DOI:https://doi.org/10.1088/1478-3975/11/4/044001
ISSN:1478-3967
ISSN:1478-3975
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/25078656
Title of parent work (English):Physical biology : a journal for the fundamental understanding of biological systems
Publisher:IOP Publ. Ltd.
Place of publishing:Bristol
Publication type:Article
Language:English
Year of first publication:2014
Publication year:2014
Release date:2017/03/27
Tag:DNA; electrostatics; nucleosome
Volume:11
Issue:4
Number of pages:6
Funding institution:Deutsche Forschungsgemeinschaft (DFG) [CH 707/5-1]; Heidelberg Center for Modeling and Simulation in the Biosciences (BIOMS); DKFZ Intramural Grant
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Physik und Astronomie
Peer review:Referiert
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