14-3-3 mediates histone cross-talk during transcription elongation in Drosophila

PLoS Genet. 2010 Jun 3;6(6):e1000975. doi: 10.1371/journal.pgen.1000975.


Post-translational modifications of histone proteins modulate the binding of transcription regulators to chromatin. Studies in Drosophila have shown that the phosphorylation of histone H3 at Ser10 (H3S10ph) by JIL-1 is required specifically during early transcription elongation. 14-3-3 proteins bind H3 only when phosphorylated, providing mechanistic insights into the role of H3S10ph in transcription. Findings presented here show that 14-3-3 functions downstream of H3S10ph during transcription elongation. 14-3-3 proteins localize to active genes in a JIL-1-dependent manner. In the absence of 14-3-3, levels of actively elongating RNA polymerase II are severely diminished. 14-3-3 proteins interact with Elongator protein 3 (Elp3), an acetyltransferase that functions during transcription elongation. JIL-1 and 14-3-3 are required for Elp3 binding to chromatin, and in the absence of either protein, levels of H3K9 acetylation are significantly reduced. These results suggest that 14-3-3 proteins mediate cross-talk between histone phosphorylation and acetylation at a critical step in transcription elongation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins / metabolism*
  • Acetylation
  • Animals
  • Chromosomes / genetics
  • Chromosomes / metabolism
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Gene Expression Regulation
  • Histone Acetyltransferases / metabolism
  • Histones / metabolism*
  • Nerve Tissue Proteins / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein-Serine-Threonine Kinases / metabolism
  • Transcription, Genetic*


  • 14-3-3 Proteins
  • Drosophila Proteins
  • Histones
  • Nerve Tissue Proteins
  • ELP3 protein, Drosophila
  • Histone Acetyltransferases
  • JIL-1 protein, Drosophila
  • Protein-Serine-Threonine Kinases