A quantitative model of nucleosome dynamics

Nucleic Acids Res. 2011 Oct;39(19):8306-13. doi: 10.1093/nar/gkr422. Epub 2011 Jul 14.

Abstract

The expression, replication and repair of eukaryotic genomes require the fundamental organizing unit of chromatin, the nucleosome, to be unwrapped and disassembled. We have developed a quantitative model of nucleosome dynamics which provides a fundamental understanding of these DNA processes. We calibrated this model using results from high precision single molecule nucleosome unzipping experiments, and then tested its predictions for experiments in which nucleosomes are disassembled by the DNA mismatch recognition complex hMSH2-hMSH6. We found that this calibrated model quantitatively describes hMSH2-hMSH6 induced disassembly rates of nucleosomes with two separate DNA sequences and four distinct histone modification states. In addition, this model provides mechanistic insight into nucleosome disassembly by hMSH2-hMSH6 and the influence of histone modifications on this disassembly reaction. This model's precise agreement with current experiments suggests that it can be applied more generally to provide important mechanistic understanding of the numerous nucleosome alterations that occur during DNA processing.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Chromatin Assembly and Disassembly*
  • DNA-Binding Proteins / metabolism
  • Histones / metabolism
  • Models, Genetic*
  • MutS Homolog 2 Protein / metabolism
  • Nucleosomes / chemistry*
  • Nucleosomes / metabolism
  • Protein Processing, Post-Translational

Substances

  • DNA-Binding Proteins
  • G-T mismatch-binding protein
  • Histones
  • Nucleosomes
  • MSH2 protein, human
  • MutS Homolog 2 Protein