RRC ID |
11090
|
著者 |
Karam CS, Kellner WA, Takenaka N, Clemmons AW, Corces VG.
|
タイトル |
14-3-3 mediates histone cross-talk during transcription elongation in Drosophila.
|
ジャーナル |
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.
|
巻・号 |
6(6)
|
ページ |
e1000975
|
公開日 |
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
|
引用数 |
39
|
WOS 分野
|
GENETICS & HEREDITY
|
リソース情報 |
ショウジョウバエ |
31196R-4 |