A plasmid model system shows that Drosophila dosage compensation depends on the global acetylation of histone H4 at lysine 16 and is not affected by depletion of common transcription elongation chromatin marks

Mol Cell Biol. 2007 Nov;27(22):7865-70. doi: 10.1128/MCB.00397-07. Epub 2007 Sep 17.

Abstract

Dosage compensation refers to the equalization of most X-linked gene products between males, which have one X chromosome and a single dose of X-linked genes, and females, which have two X's and two doses of such genes. We developed a plasmid-based model of dosage compensation that allows new experimental approaches for the study of this regulatory mechanism. In Drosophila melanogaster, an enhanced rate of transcription of the X chromosome in males is dependent upon the presence of histone H4 acetylated at lysine 16. This chromatin mark occurs throughout active transcriptional units, leading us to the conclusion that the enhanced level of transcription is achieved through an enhanced rate of RNA polymerase elongation. We used the plasmid model to demonstrate that enhancement in the level of transcription does not depend on other histone marks and factors that have been associated with the process of elongation, thereby highlighting the special role played by histone H4 acetylated at lysine 16 in this process.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylation
  • Animals
  • Chromatin* / genetics
  • Chromatin* / metabolism
  • Dosage Compensation, Genetic*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / genetics*
  • Drosophila melanogaster / metabolism
  • Female
  • Gene Expression Regulation*
  • Genes, Reporter
  • Histone Deacetylases / genetics
  • Histone Deacetylases / metabolism
  • Histones / genetics
  • Histones / metabolism*
  • Lysine / metabolism*
  • Male
  • Plasmids* / genetics
  • Plasmids* / metabolism
  • Promoter Regions, Genetic
  • RNA Interference
  • X Chromosome / genetics

Substances

  • Chromatin
  • Drosophila Proteins
  • Histones
  • Histone Deacetylases
  • Lysine