Phosphorylation of histone H3 correlates with transcriptionally active loci

Abstract

Posttranslational modifications of the N-terminal tails of the core histones within the nucleosome particle are thought to act as signals from the chromatin to the cell for various processes. The experiments presented here show that the acetylation of histones H3 and H4 in polytene chromosomes does not change during heat shock. In contrast, the global level of phosphorylated H3 decreased dramatically during a heat shock, with an observed increase in H3 phosphorylation at the heat shock loci. Additional experiments confirm that this change in phosphorylated H3 distribution is dependent on functional heat shock transcription factor activity. These experiments suggest that H3 phosphorylation has an important role in the induction of transcription during the heat shock response.

Phosphorylation of histone H3 during transcriptional activation depends on promoter structure

“…This association correlates with transcription activation and is supported as well by structural data showing a specific interaction between arginine 164 of GCN5 and the phosphorylated Ser 10 of the H3 N-terminal tail. Other results, however, question the general implication of this model when applied to other organisms; for example, the dramatic changes in H3 phosphorylation that take place during the heat shock response in Drosophila are not followed by equivalent changes in histone acetylation (Nowak and Corces 2000). The histone H3 N-terminal tails at the Drosophila heat shock genes become hyperphosphorylated at Ser 10 upon induction of transcription by heat shock.…”

“…In addition, phosphorylated histone H3 disappears from all nonheat shock loci during the heat shock response, coinciding with the shutdown of transcription of most genes, further supporting the hypothesis that H3 phosphorylation may have a central role in the control of gene expression in Drosophila. Except for a weak acetylation signal in some of the heat Cold Spring Harbor Laboratory Press on May 10, 2018 -Published by genesdev.cshlp.org Downloaded from shock puffs, the global changes observed in H3 phosphorylation after heat shock are not followed by detectable equivalent changes in H3 or H4 acetylation (Nowak and Corces 2000).To gain further insights into the role of H3 phosphorylation during transcription in Drosophila and its correlation with acetylation, we addressed the question of whether phosphorylation and acetylation at specific residues of the histone N-terminal tails are associated with transcription of transgenes ectopically activated by the Gal4 transcriptional activator. In yeast, the acidic domains of the widely used exogenous transcriptional activators Gal4 and VP16 recruit the SAGA complex to the promoter of the gene (Bhaumik and Green 2001;Larschan and Winston 2001).…”

“…H3 methylation at Lys 9 has the opposite effect and therefore is found in regions where transcription is repressed by chromatin structure (Rea et al 2000;Bannister et al 2001). Phosphorylation of H3 at Ser 10 has also been correlated with activation of transcription in yeast, mammals, and Drosophila (Cheung et al 2000;Lo et al 2000;Nowak and Corces 2000;Lo et al 2001;Thomson et al 2001;Li et al 2002;Strelkov and Davie 2002).Two nonexclusive models have been postulated to explain the role of histone N-terminal tail modification in transcription. The first one suggests that histone modifications have an effect on the relative charge of the histone tails, rendering a more open or closed chromatin state that determines the accessibility of transcription factors to the core promoter.…”

BMP signaling mutant mice exhibit glial cell maturation defects

“…To determine extent of cell proliferation, sections were immunolabeled separately with antibody to the mitosis marker phosphorylated histone H3 and with antibody to the proliferation protein Ki-67 (Hendzel et al, 1997;Nowak and Corces, 2000;Scholzen and Gerdes, 2000). Sections were processed as described above and incubated in anti-phospho-histone 3 antibody (1:250 in block, Upstate Biotechnology) or Ki-67 antibody (1:100.…”

Re-expression of DNA methylation-silenced CD44 gene in a resistant NB4 cell line: rescue of CD44-dependent cell death by cAMP

“…Current hypotheses suggest that histone modifications on the terminal tails, including acetylation, methylation and phosphorylation, constituting a code, are crucial steps in controlling transcription of genes. [32][33][34] As mentioned above, in addition to acetylation of lysine residues, histone H3 phosphorylation of Ser10 or phospho-acetylation of Ser10, Lys14 are shown associated with active loci, [35][36][37] while methylation of lysine 9 in histone H3 is associated with silent loci. [38][39][40][41] ChIP experiments specifically performed at the CD44 locus with anti-acetyl Lys9;Lys14 (H3AcK9;K14) or anti-phospho-acetyl Ser10;Lys14 (H3pS10AcK14) histone H3 antibodies did not reveal any change in histone H3 tail modifications after cAMP treatment (Figure 4b).…”