Functional interplay between histone H1 and HMG proteins in chromatin

Biochim Biophys Acta. 2016 Mar;1859(3):462-7. doi: 10.1016/j.bbagrm.2015.10.006. Epub 2015 Oct 8.

Abstract

The dynamic interaction of nucleosome binding proteins with their chromatin targets is an important element in regulating the structure and function of chromatin. Histone H1 variants and High Mobility Group (HMG) proteins are ubiquitously expressed in all vertebrate cells, bind dynamically to chromatin, and are known to affect chromatin condensation and the ability of regulatory factors to access their genomic binding sites. Here, we review the studies that focus on the interactions between H1 and HMGs and highlight the functional consequences of the interplay between these architectural chromatin binding proteins. H1 and HMG proteins are mobile molecules that bind to nucleosomes as members of a dynamic protein network. All HMGs compete with H1 for chromatin binding sites, in a dose dependent fashion, but each HMG family has specific effects on the interaction of H1 with chromatin. The interplay between H1 and HMGs affects chromatin organization and plays a role in epigenetic regulation.

Keywords: Chromatin; HMG proteins; Histone H1.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Animals
  • Carrier Proteins / physiology
  • Chromatin / chemistry*
  • High Mobility Group Proteins / physiology*
  • Histones / physiology*
  • Humans

Substances

  • Carrier Proteins
  • Chromatin
  • High Mobility Group Proteins
  • Histones