Nucleosome adaptability conferred by sequence and structural variations in histone H2A-H2B dimers

Curr Opin Struct Biol. 2015 Jun;32:48-57. doi: 10.1016/j.sbi.2015.02.004. Epub 2015 Feb 27.

Abstract

Nucleosome variability is essential for their functions in compacting the chromatin structure and regulation of transcription, replication and cell reprogramming. The DNA molecule in nucleosomes is wrapped around an octamer composed of four types of core histones (H3, H4, H2A, H2B). Nucleosomes represent dynamic entities and may change their conformation, stability and binding properties by employing different sets of histone variants or by becoming post-translationally modified. There are many variants of histones H2A and H2B. Specific H2A and H2B variants may preferentially associate with each other resulting in different combinations of variants and leading to the increased combinatorial complexity of nucleosomes. In addition, the H2A-H2B dimer can be recognized and substituted by chaperones/remodelers as a distinct unit, can assemble independently and is stable during nucleosome unwinding. In this review we discuss how sequence and structural variations in H2A-H2B dimers may provide necessary complexity and confer the nucleosome functional variability.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Evolution, Molecular
  • Histones / chemistry*
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleosomes / chemistry*
  • Nucleosomes / genetics
  • Nucleosomes / metabolism*
  • Protein Conformation
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein Multimerization
  • Protein Stability
  • Sequence Alignment

Substances

  • Histones
  • Nucleosomes
  • Protein Isoforms