Published August 2014 | Version v1
Journal article

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

  • 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/10.1088/1478-3975/11/4/044001

Additional details

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