Histone H4-lysine 20 monomethylation is increased in promoter and coding regions of active genes and correlates with hyperacetylation

J Biol Chem. 2005 Nov 18;280(46):38814-22. doi: 10.1074/jbc.M505563200. Epub 2005 Sep 15.

Abstract

Methylation and acetylation of position-specific lysine residues in the N-terminal tail of histones H3 and H4 play an important role in regulating chromatin structure and function. In the case of H3-Lys(4), H3-Lys(9), H3-Lys(27), and H4-Lys(20), the degree of methylation was variable from the mono- to the di- or trimethylated state, each of which was presumed to be involved in the organization of chromatin and the activation or repression of genes. Here we investigated the interplay between histone H4-Lys(20) mono- and trim-ethylation and H4 acetylation at induced (beta-major/beta-minor glo-bin), repressed (c-myc), and silent (embryonic beta-globin) genes during in vitro differentiation of mouse erythroleukemia cells. By using chromatin immunoprecipitation, we found that the beta-major and beta-minor promoter and the beta-globin coding regions as well as the promoter and the transcribed exon 2 regions of the highly expressed c-myc gene were hyperacetylated and monomethylated at H4-Lys(20). Although activation of the beta-globin gene resulted in an increase in hyperacetylated, monomethylated H4, down-regulation of the c-myc gene did not cause a decrease in hyperacetylated, monomethylated H4-Lys(20), thus showing a stable pattern of histone modifications. Immunofluorescence microscopy studies revealed that monomethylated H4-Lys(20) mainly overlaps with RNA pol II-stained euchromatic regions, thus indicating an association with transcriptionally engaged chromatin. Our chromatin immunoprecipitation results demonstrated that in contrast to trimethylated H4-Lys(20), which was found to inversely correlate with H4 hyper-acetylation, H4-Lys(20) monomethylation is compatible with histone H4 hyperacetylation and correlates with the transcriptionally active or competent chromatin state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Blotting, Western
  • Butyrates / pharmacology
  • Cell Differentiation
  • Cell Line
  • Cell Line, Tumor
  • Chromatin / chemistry
  • Chromatin Immunoprecipitation
  • Chromatography, Liquid
  • Cross-Linking Reagents / pharmacology
  • Down-Regulation
  • Exons
  • Formaldehyde / pharmacology
  • Globins / chemistry
  • Heterochromatin / chemistry
  • Histones / chemistry*
  • Immunoprecipitation
  • Isobutyrates
  • Lysine / chemistry*
  • Methylation
  • Mice
  • Microscopy, Fluorescence
  • Polymerase Chain Reaction
  • Protein Binding
  • Proto-Oncogene Proteins c-myc / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Time Factors
  • Transcription, Genetic

Substances

  • Butyrates
  • Chromatin
  • Cross-Linking Reagents
  • Heterochromatin
  • Histones
  • Isobutyrates
  • Proto-Oncogene Proteins c-myc
  • Formaldehyde
  • isobutyric acid
  • Globins
  • Lysine