Recognizing and remodeling the nucleosome

Curr Opin Struct Biol. 2011 Jun;21(3):335-41. doi: 10.1016/j.sbi.2011.02.003. Epub 2011 Mar 4.

Abstract

The X-ray structure of the nucleosome core particle (NCP) has been a major milestone in the structural biology of chromatin. Since, our understanding how NCPs interact with multiple partners has been extending from single chromatin-binding domains recognizing post-translational modifications (PTMs) in histone tails towards the recognition of higher-order chromatin structure by multi-subunit chromatin remodeling complexes. The current review summarizes recent progress in the structural biology of nucleosome-recognition from chromatin-binding domains to multi-protein remodeling complexes.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Chromatin Assembly and Disassembly*
  • DNA / chemistry
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Humans
  • Ligands
  • Models, Molecular
  • Nucleoproteins / chemistry
  • Nucleoproteins / metabolism
  • Nucleosomes* / chemistry
  • Nucleosomes* / genetics
  • Nucleosomes* / metabolism
  • Protein Binding / physiology

Substances

  • DNA-Binding Proteins
  • Ligands
  • Nucleoproteins
  • Nucleosomes
  • Adenosine Triphosphate
  • DNA