Histone variants in pluripotency and disease

Development. 2013 Jun;140(12):2513-24. doi: 10.1242/dev.091439.

Abstract

Most histones are assembled into nucleosomes during replication to package genomic DNA. However, several variant histones are deposited independently of replication at particular regions of chromosomes. Such histone variants include cenH3, which forms the nucleosomal foundation for the centromere, and H3.3, which replaces histones that are lost during dynamic processes that disrupt nucleosomes. Furthermore, various H2A variants participate in DNA repair, gene regulation and other processes that are, as yet, not fully understood. Here, we review recent studies that have implicated histone variants in maintaining pluripotency and as causal factors in cancer and other diseases.

Keywords: Disease; Histone chaperone; Histone variant; Nucleosome dynamics; Reprogramming.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cellular Reprogramming
  • Chromatin / genetics
  • Chromatin / metabolism
  • DNA Helicases / genetics
  • DNA Helicases / metabolism
  • Disease Progression
  • Embryonic Stem Cells / metabolism*
  • Embryonic Stem Cells / pathology
  • Epigenesis, Genetic
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Neoplasms / genetics
  • Neoplasms / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Nucleosomes / genetics
  • Nucleosomes / metabolism*
  • Octamer Transcription Factor-3 / genetics
  • Octamer Transcription Factor-3 / metabolism
  • Pluripotent Stem Cells / metabolism*
  • X-linked Nuclear Protein

Substances

  • Chromatin
  • Histones
  • Nuclear Proteins
  • Nucleosomes
  • Octamer Transcription Factor-3
  • POU5F1 protein, human
  • DNA Helicases
  • ATRX protein, human
  • X-linked Nuclear Protein