Histone 1 is proximal to histone 2A and to A24

Proc Natl Acad Sci U S A. 1979 May;76(5):2190-4. doi: 10.1073/pnas.76.5.2190.

Abstract

Water-soluble carbodiimide crosslinks histones 1A and 1B to histone 2A and to semi-histone A24 in chromatin from mouse cells. The identities of the histone species present in the crosslinked dimers were determined by fingerprinting. The molar ratio of H1--A24 to H2A is the same as the molar ratio of A24 to H2A in these cells. The H1-H2A crosslinks form equally well in whole nuclei, lysed nuclei, and H1-containing mononucleosomes isolated from a sucrose gradient. These results suggest that there exist major H1 interactions within the nucleosome.

MeSH terms

  • Animals
  • Binding Sites
  • Carbodiimides
  • Cell Nucleus / ultrastructure
  • Chickens
  • Chromatin / ultrastructure*
  • Chromosomal Proteins, Non-Histone / metabolism
  • DNA / metabolism
  • Erythrocytes / ultrastructure
  • Histones* / metabolism*
  • Leukemia L1210
  • Mice
  • Protein Binding
  • Protein Conformation

Substances

  • Carbodiimides
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • Histones
  • DNA