RRC ID 11090
Author Karam CS, Kellner WA, Takenaka N, Clemmons AW, Corces VG.
Title 14-3-3 mediates histone cross-talk during transcription elongation in Drosophila.
Journal PLoS Genet
Abstract 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.
Volume 6(6)
Pages e1000975
Published 2010-6-3
DOI 10.1371/journal.pgen.1000975
PMID 20532201
PMC PMC2880557
MeSH 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*
IF 5.175
Times Cited 39
WOS Category GENETICS & HEREDITY
Resource
Drosophila 31196R-4