Electrostatic effect of H1-histone protein binding on nucleosome repeat length
Creators
- 1. Institute for Physics and Astronomy, University of Potsdam, 14476 Potsdam-Golm (Germany)
- 2. Deutsches Krebsforschungszentrum (DKFZ) and BioQuant, 69120 Heidelberg (Germany)
Description
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. (note)
Availability note (English)
Available from http://dx.doi.org/10.1088/1478-3975/11/4/044001Additional details
Identifiers
Publishing Information
- Journal Title
- Physical Biology (Online)
- Journal Volume
- 11
- Journal Issue
- 4
- Journal Page Range
- [6 p.]
- ISSN
- 1478-3975
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 47050689
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- BINDING ENERGY; BIOLOGICAL MODELS; COMPARATIVE EVALUATIONS; DNA; FIBERS; HISTONES; LENGTH; NUCLEOSOMES; POSITIONING; VARIATIONS
- Descriptors DEC
- CHROMATIN; DIMENSIONS; ENERGY; EVALUATION; NUCLEIC ACIDS; ORGANIC COMPOUNDS; PROTEINS