Specific variants of H1 histone regulate CpG methylation in eukaryotic DNA

Gene. 1995 May 19;157(1-2):253-6. doi: 10.1016/0378-1119(95)91236-s.

Abstract

Upon HPLC fractionation of human placenta or calf thymus H1 histone preparations, only some fractions enriched in the H1e-c variants were able to exert a severe inhibition on in vitro enzymatic DNA methylation. These fractions, though similar to the other variants in interacting with genomic DNA, were also the only ones which could bind CpG-rich ds-oligodeoxyribonucleotides (oligos). Both the 6-CpG ds-oligo and the DNA purified from chromatin fractions enriched in 'CpG islands' were good competitors for the binding of H1e-c to the 6meCpG ds-oligo. This ability to bind any DNA sequence and to suppress the enzymatic methylation in any sequence containing CpG dinucleotides suggests, for these particular H1 variants, a possible role in maintaining CpG island DNA and linker DNA at low methylation levels.

Publication types

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

MeSH terms

  • Animals
  • Base Sequence
  • Cattle
  • Chromatin / chemistry
  • Chromatin / metabolism
  • DNA / chemistry
  • DNA / isolation & purification
  • DNA / metabolism*
  • Dinucleoside Phosphates
  • Female
  • Genetic Variation*
  • Histones / genetics*
  • Histones / isolation & purification
  • Histones / metabolism*
  • Humans
  • Methylation
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / chemical synthesis
  • Oligodeoxyribonucleotides / chemistry*
  • Oligodeoxyribonucleotides / metabolism
  • Placenta / metabolism
  • Pregnancy
  • Thymus Gland / metabolism

Substances

  • Chromatin
  • Dinucleoside Phosphates
  • Histones
  • Oligodeoxyribonucleotides
  • cytidylyl-3'-5'-guanosine
  • DNA