The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization

J Biol Chem. 2011 May 27;286(21):18369-74. doi: 10.1074/jbc.R110.180778. Epub 2011 Mar 24.

Abstract

Changes in chromatin architecture induced by epigenetic mechanisms are essential for normal cellular processes such as gene expression, DNA repair, and cellular division. Compact chromatin presents a barrier to these processes and is highly regulated by epigenetic markers binding to components of the nucleosome. Histone modifications directly influence chromatin dynamics and facilitate recruitment of additional factors such as chromatin remodelers and histone chaperones. One member of this last class of factors, FACT (facilitates chromatin transcription), is categorized as a histone chaperone critical for nucleosome reorganization during replication, transcription, and DNA repair. Significant discoveries regarding the role of histone chaperones and specifically FACT have come over the past dozen years from a number of independent laboratories. Here, we review the structural and biophysical basis for FACT-mediated nucleosome reorganization and discuss up-to-date models for FACT function.

Publication types

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

MeSH terms

  • Animals
  • Chromatin Assembly and Disassembly / physiology*
  • DNA Repair / physiology
  • DNA Replication / physiology
  • DNA-Binding Proteins / metabolism*
  • High Mobility Group Proteins / metabolism*
  • Histones / metabolism*
  • Humans
  • Models, Biological*
  • Molecular Chaperones / metabolism*
  • Nucleosomes / metabolism*
  • Structure-Activity Relationship
  • Transcription, Genetic / physiology
  • Transcriptional Elongation Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • Histones
  • Molecular Chaperones
  • Nucleosomes
  • SSRP1 protein, human
  • Transcriptional Elongation Factors