Structural dynamics of nucleosomes at single-molecule resolution

Trends Biochem Sci. 2012 Oct;37(10):425-35. doi: 10.1016/j.tibs.2012.06.006. Epub 2012 Jul 23.

Abstract

The detailed mechanisms of how DNA that is assembled around a histone core can be accessed by DNA-binding proteins for transcription, replication, or repair, remain elusive nearly 40 years after Kornberg's nucleosome model was proposed. Uncovering the structural dynamics of nucleosomes is a crucial step in elucidating the mechanisms regulating genome accessibility. This requires the deconvolution of multiple structural states within an ensemble. Recent advances in single-molecule methods enable unprecedented efficiency in examining subpopulation dynamics. In this review, we summarize studies of nucleosome structure and dynamics from single-molecule approaches and how they advance our understanding of the mechanisms that govern DNA transactions.

Publication types

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

MeSH terms

  • DNA / chemistry
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Humans
  • Models, Molecular
  • Nucleic Acid Conformation
  • Nucleosomes / chemistry*
  • Nucleosomes / metabolism*

Substances

  • DNA-Binding Proteins
  • Nucleosomes
  • DNA