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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z.

Activation of transcription within chromatin has been correlated with the incorporation of the essential histone variant H2A.Z into nucleosomes. H2A.Z and other histone variants may establish structurally distinct chromosomal domains; however, the molecular mechanism by which they function is largely unknown. Here we report the 2.6 A crystal structure of a nucleosome core particle containing the histone variant H2A.Z. The overall structure is similar to that of the previously reported 2.8 A nucleosome structure containing major histone proteins. However, distinct localized changes result in the subtle destabilization of the interaction between the (H2A.Z-H2B) dimer and the (H3-H4)(2) tetramer. Moreover, H2A.Z nucleosomes have an altered surface that includes a metal ion. This altered surface may lead to changes in higher order structure, and/or could result in the association of specific nuclear proteins with H2A.Z. Finally, incorporation of H2A.Z and H2A within the same nucleosome is unlikely, due to significant changes in the interface between the two H2A.Z-H2B dimers.

Pubmed ID: 11101893

Authors

  • Suto RK
  • Clarkson MJ
  • Tremethick DJ
  • Luger K

Journal

Nature structural biology

Publication Data

December 27, 2000

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Dimerization
  • Genetic Variation
  • Histones
  • Metals
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleosomes
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Static Electricity
  • Xenopus laevis