scholarly journals The Essential Gene wda Encodes a WD40 Repeat Subunit of Drosophila SAGA Required for Histone H3 Acetylation

2006 ◽  
Vol 26 (19) ◽  
pp. 7178-7189 ◽  
Author(s):  
Sebastián Guelman ◽  
Tamaki Suganuma ◽  
Laurence Florens ◽  
Vikki Weake ◽  
Selene K. Swanson ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Essential Gene ◽  
Histone H3 ◽  
The Novel ◽  
Critical Function ◽  
High Molecular Weight Complex ◽  
Proteomic Approach ◽  
Histone H3 Acetylation ◽  
H3 Acetylation ◽  
Novel Protein

ABSTRACT Histone acetylation provides a switch between transcriptionally repressive and permissive chromatin. By regulating the chromatin structure at specific promoters, histone acetyltransferases (HATs) carry out important functions during differentiation and development of higher eukaryotes. HAT complexes are present in organisms as diverse as Saccharomyces cerevisiae, humans, and flies. For example, the well-studied yeast SAGA is related to three mammalian complexes. We previously identified Drosophila melanogaster orthologues of yeast SAGA components Ada2, Ada3, Spt3, and Tra1 and demonstrated that they associate with dGcn5 in a high-molecular-weight complex. To better understand the function of Drosophila SAGA (dSAGA), we sought to affinity purify and characterize this complex in more detail. A proteomic approach led to the identification of an orthologue of the yeast protein Ada1 and the novel protein encoded by CG4448, referred to as WDA (will decrease acetylation). Embryos lacking both alleles of the wda gene exhibited reduced levels of histone H3 acetylation and could not develop into adult flies. Our results point to a critical function of dSAGA and histone acetylation during Drosophila development.

Differential histone acetylation in the Amygdala leads to fear memory consolidation and extinction

2015 ◽  
Vol 1 (1) ◽  
Author(s):  
Vandana Ranjan ◽  
Sanjay Singh ◽  
Sarfraj Ahmad Siddiqui ◽  
M Y Khan ◽  
Anand Prakash
Keyword(s):  
Histone Acetylation ◽  
Memory Consolidation ◽  
Histone H3 ◽  
Fear Memory ◽  
Memory Formation ◽  
Acetylation Level ◽  
Creb Activation ◽  
Conditioning Model ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

<p>In the present study, a fear-conditioning model in rats was used to gauge the changes in the histone acetylation level in the<br />different nuclei of amygdala during fear memory consolidation and its extinction. It was found by immunohistochemical<br />examination of Amygdala that during the fear memory consolidation histone H3 acetylation level was significantly<br />increased in the Central amygdala (CeA), the output of the fear circuitry, as compared to the unconditioned group and<br />subsequently, when this fear memory was extinguished during fear extinction, the histone H3 acetylation levels decreased<br />significantly as compared to the conditioned group. However, in another nuclei of the amygdala, the intercalated cells<br />(ITCs) the Acetyl H3 levels increased during extinction and but not in the conditioned group as compared to the<br />unconditioned group. The p-ERK and p-CREB levels also significantly varied in the different nuclei of amygdala<br />between the two groups and showed correlation with the Histone acetylation changes observed in these groups. In<br />conclusion the present study points out that the memory formation, during fear memory consolidation and its extinction,<br />may be dependent on differential neuronal activity under epigenetic control through acetylation at k-9 residue of histone<br />H3, in different regions of the amygdala as evident by the p-ERK and p-CREB activation, which are the markers for<br />activity of neurons and memory formation.</p>

scholarly journals H4R3 methylation facilitates β-globin transcription by regulating histone acetyltransferase binding and H3 acetylation

Blood ◽  
2010 ◽  
Vol 115 (10) ◽  
pp. 2028-2037 ◽  
Author(s):  
Xingguo Li ◽  
Xin Hu ◽  
Bhavita Patel ◽  
Zhuo Zhou ◽  
Shermi Liang ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Chromatin Structure ◽  
Globin Gene ◽  
Histone H3 ◽  
Arginine Methylation ◽  
Globin Genes ◽  
Erythroid Progenitor ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Abstract Histone modifications play an important role in the process of transcription. However, in contrast to lysine methylation, the role of arginine methylation in chromatin structure and transcription has been underexplored. The globin genes are regulated by a highly organized chromatin structure that juxtaposes the locus control region (LCR) with downstream globin genes. We report here that the targeted recruitment of asymmetric dimethyl H4R3 catalyzed by PRMT1 (protein arginine methyltransferase 1) facilitates histone H3 acetylation on Lys9/Lys14. Dimethyl H4R3 provides a binding surface for P300/CBP-associated factor (PCAF) and directly enhances histone H3 acetylation in vitro. We show that these active modifications are essential for efficient interactions between the LCR and the βmaj-promoter as well as transcription of the β-globin gene. Furthermore, knockdown (KD) of PRMT1 by RNA interference in erythroid progenitor cells prevents histone acetylation, enhancer and promoter interaction, and recruitment of transcription complexes to the active β-globin promoter. Reintroducing rat PRMT1 into the PRMT1 KD MEL cells rescues PRMT1 binding, β-globin transcription, and erythroid differentiation. Taken together, our data suggest that PRMT1-mediated dimethyl H4R3 facilitates histone acetylation and enhancer/promoter communications, which lead to the efficient recruitment of transcription preinitiation complexes to active promoters.

scholarly journals Butyrate Stimulates Histone H3 Acetylation, 8-Isoprostane Production, RANKL Expression, and Regulated Osteoprotegerin Expression/Secretion in MG-63 Osteoblastic Cells

2018 ◽  
Vol 19 (12) ◽  
pp. 4071 ◽  
Author(s):  
Mei-Chi Chang ◽  
Yunn-Jy Chen ◽  
Yun-Chia Lian ◽  
Bei-En Chang ◽  
Chih-Chia Huang ◽  
...  
Keyword(s):  
Protein Expression ◽  
Cell Viability ◽  
Butyric Acid ◽  
Root Canal ◽  
Histone H3 ◽  
Rankl Expression ◽  
Alp Activity ◽  
Histone H3 Acetylation ◽  
Apoptosis And Necrosis ◽  
H3 Acetylation

Butyric acid as a histone deacetylase (HDAC) inhibitor is produced by a number of periodontal and root canal microorganisms (such as Porphyromonas, Fusobacterium, etc.). Butyric acid may affect the biological activities of periodontal/periapical cells such as osteoblasts, periodontal ligament cells, etc., and thus affect periodontal/periapical tissue destruction and healing. The purposes of this study were to study the toxic effects of butyrate on the matrix and mineralization marker expression in MG-63 osteoblasts. Cell viability was determined by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) assay. Cellular apoptosis and necrosis were analyzed by propidium iodide/annexin V flow cytometry. The protein and mRNA expression of osteoprotegerin (OPG) and receptor activator of nuclear factor kappa-B ligand (RANKL) were analyzed by Western blotting and reverse transcriptase-polymerase chain reaction (RT-PCR). OPG, soluble RANKL (sRANKL), 8-isoprostane, pro-collagen I, matrix metalloproteinase-2 (MMP-2), osteonectin (SPARC), osteocalcin and osteopontin (OPN) secretion into culture medium were measured by enzyme-linked immunosorbant assay. Alkaline phosphatase (ALP) activity was checked by ALP staining. Histone H3 acetylation levels were evaluated by immunofluorescent staining (IF) and Western blot. We found that butyrate activated the histone H3 acetylation of MG-63 cells. Exposure of MG-63 cells to butyrate partly decreased cell viability with no marked increase in apoptosis and necrosis. Twenty-four hours of exposure to butyrate stimulated RANKL protein expression, whereas it inhibited OPG protein expression. Butyrate also inhibited the secretion of OPG in MG-63 cells, whereas the sRANKL level was below the detection limit. However, 3 days of exposure to butyrate (1 to 8 mM) or other HDAC inhibitors such as phenylbutyrate, valproic acid and trichostatin stimulated OPG secretion. Butyrate stimulated 8-isoprostane, MMP-2 and OPN secretion, but not procollagen I, or osteocalcin in MG-63 cells. Exposure to butyrate (2–4 mM) for 3 days markedly stimulated osteonectin secretion and ALP activity. In conclusion, higher concentrations of butyric acid generated by periodontal and root canal microorganisms may potentially induce bone destruction and impair bone repair by the alteration of OPG/RANKL expression/secretion, 8-isoprostane, MMP-2 and OPN secretion, and affect cell viability. However, lower concentrations of butyrate (1–4 mM) may stimulate ALP, osteonectin and OPG. These effects are possibly related to increased histone acetylation. These events are important in the pathogenesis and repair of periodontal and periapical destruction.

scholarly journals Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation

2011 ◽  
Vol 30 (14) ◽  
pp. 2829-2842 ◽  
Author(s):  
Chuanbing Bian ◽  
Chao Xu ◽  
Jianbin Ruan ◽  
Kenneth K Lee ◽  
Tara L Burke ◽  
...  
Keyword(s):  
Histone H3 ◽  
Saga Complex ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals Promoter-specific changes in initiation, elongation and homeostasis of histone H3 acetylation during CBP/p300 inhibition

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Emily Hsu ◽  
Nathan R Zemke ◽  
Arnold J Berk
Keyword(s):  
Rna Polymerase Ii ◽  
Control Point ◽  
Histone H3 ◽  
Airway Epithelial Cells ◽  
Proximal Region ◽  
Transferase Activity ◽  
Transcriptional Elongation ◽  
Elongation Complex ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Regulation of RNA Polymerase II (Pol2) elongation in the promoter proximal region is an important and ubiquitous control point for gene expression in metazoans. We report that transcription of the adenovirus 5 E4 region is regulated during the release of paused Pol2 into productive elongation by recruitment of the super elongation complex (SEC), dependent on promoter H3K18/27 acetylation by CBP/p300. We also establish that this is a general transcriptional regulatory mechanism that applies to ~6% of expressed protein-coding genes in primary human airway epithelial cells. We observed that a homeostatic mechanism maintains promoter, but not enhancer H3K18/27ac in response to extensive inhibition of CBP/p300 acetyl transferase activity by the highly specific small molecule inhibitor A-485. Further, our results suggest a function for BRD4 association at enhancers in regulating paused Pol2 release at nearby promoters. Taken together, our results uncover processes regulating transcriptional elongation by promoter region histone H3 acetylation and homeostatic maintenance of promoter, but not enhancer, H3K18/27ac in response to inhibition of CBP/p300 acetyl transferase activity.

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