scholarly journals Brd4’s Bromodomains Mediate Histone H3 Acetylation and Chromatin Remodeling in Pluripotent Cells through P300 and Brg1

Cell Reports ◽  
2018 ◽  
Vol 25 (7) ◽  
pp. 1756-1771 ◽  
Author(s):  
Tao Wu ◽  
Yasunao F. Kamikawa ◽  
Mary E. Donohoe
Keyword(s):  
Chromatin Remodeling ◽  
Histone H3 ◽  
Pluripotent Cells ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals Acetylation of Rsc4p by Gcn5p Is Essential in the Absence of Histone H3 Acetylation

2008 ◽  
Vol 28 (23) ◽  
pp. 6967-6972 ◽  
Author(s):  
Jennifer K. Choi ◽  
Daniel E. Grimes ◽  
Keegan M. Rowe ◽  
LeAnn J. Howe
Keyword(s):  
Chromatin Remodeling ◽  
Histone H3 ◽  
Growth Defect ◽  
Chromatin Remodeling Complex ◽  
Histone H3 Acetylation ◽  
Phenotype Comparison ◽  
A Subunit ◽  
Redundant Functions ◽  
H3 Acetylation ◽  
First Time

ABSTRACT Rsc4p, a subunit of the RSC chromatin-remodeling complex, is acetylated at lysine 25 by Gcn5p, a well-characterized histone acetyltransferase (HAT). Mutation of lysine 25 does not result in a significant growth defect, and therefore whether this modification is important for the function of the essential RSC complex was unknown. In a search to uncover the molecular basis for the lethality resulting from loss of multiple histone H3-specific HATs, we determined that loss of Rsc4p acetylation is lethal in strains lacking histone H3 acetylation. Phenotype comparison of mutants with arginine and glutamine substitutions of acetylatable lysines within the histone H3 tail suggests that it is a failure to neutralize the charge of the H3 tail that is lethal in strains lacking Rsc4p acetylation. We also demonstrate that Rsc4p acetylation does not require any of the known Gcn5p-dependent HAT complexes and thus represents a truly novel function for Gcn5p. These results demonstrate for the first time the vital and yet redundant functions of histone H3 and Rsc4p acetylation in maintaining cell viability.

Reduction in Histone H3 Acetylation and Chromatin Remodeling in Corneas of Alloxan-Induced Diabetic Rats

Cornea ◽  
2018 ◽  
Vol 37 (5) ◽  
pp. 624-632 ◽  
Author(s):  
Karina E. Herencia-Bueno ◽  
Marcela Aldrovani ◽  
Roberta M. Crivelaro ◽  
Roberto Thiesen ◽  
Alexandre A. F. Barros-Sobrinho ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Histone H3 ◽  
Diabetic Rats ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals α-Synuclein A53T Binds to Transcriptional Adapter 2-Alpha and Blocks Histone H3 Acetylation

2021 ◽  
Vol 22 (10) ◽  
pp. 5392
Author(s):  
Ji-Yeong Lee ◽  
Hanna Kim ◽  
Areum Jo ◽  
Rin Khang ◽  
Chi-Hu Park ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Chromatin Remodeling ◽  
Dopaminergic Neurons ◽  
Histone H3 ◽  
Lewy Bodies ◽  
Wild Type ◽  
Binding Partner ◽  
Amyloidogenic Protein ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

α-Synuclein (α-syn) is a hallmark amyloidogenic protein component of Lewy bodies in dopaminergic neurons affected by Parkinson’s disease (PD). Despite the multi-faceted gene regulation of α-syn in the nucleus, the mechanism underlying α-syn crosstalk in chromatin remodeling in PD pathogenesis remains elusive. Here, we identified transcriptional adapter 2-alpha (TADA2a) as a novel binding partner of α-syn using the BioID system. TADA2a is a component of the p300/CBP-associated factor and is related to histone H3/H4 acetylation. We found that α-syn A53T was more preferentially localized in the nucleus than the α-syn wild-type (WT), leading to a stronger disturbance of TADA2a. Indeed, α-syn A53T significantly reduced the level of histone H3 acetylation in SH-SY5Y cells; its reduction was also evident in the striatum (STR) and substantia nigra (SN) of mice that were stereotaxically injected with α-syn preformed fibrils (PFFs). Interestingly, α-syn PFF injection resulted in a decrease in TADA2a in the STR and SN of α-syn PFF-injected mice. Furthermore, the levels of TADA2a and acetylated histone H3 were significantly decreased in the SN of patients with PD. Therefore, histone modification through α-syn A53T-TADA2a interaction may be associated with α-syn-mediated neurotoxicity in PD pathology.

scholarly journals Displacement of Histones at Promoters of Saccharomyces cerevisiae Heat Shock Genes Is Differentially Associated with Histone H3 Acetylation

2006 ◽  
Vol 26 (20) ◽  
pp. 7587-7600 ◽  
Author(s):  
T. Y. Erkina ◽  
A. M. Erkine
Keyword(s):  
Heat Shock ◽  
Chromatin Remodeling ◽  
Histone H3 ◽  
Heat Shock Gene ◽  
Gene Promoters ◽  
Heat Shock Genes ◽  
Factors Affecting ◽  
Histone H3 Acetylation ◽  
Shock Gene ◽  
H3 Acetylation

ABSTRACT Chromatin remodeling at promoters of activated genes spans from mild histone modifications to outright displacement of nucleosomes in trans. Factors affecting these events are not always clear. Our results indicate that histone H3 acetylation associated with histone displacement differs drastically even between promoters of such closely related heat shock genes as HSP12, SSA4, and HSP82. The HSP12 promoter, with the highest level of histone displacement, showed the highest level of H3 acetylation, while the SSA4 promoter, with a lower histone displacement, showed only modest H3 acetylation. Moreover, for the HSP12 promoter, the level of acetylated H3 is temporarily increased prior to nucleosome departure. Individual promoters in strains expressing truncated versions of heat shock factor (HSF) showed that deletion of either one of two activating regions in HSF led to the diminished histone displacement and correspondingly lower H3 acetylation. The deletion of both regions simultaneously severely decreased histone displacement for all promoters tested, showing the dependence of these processes on HSF. The level of histone H3 acetylation at individual promoters in strains expressing truncated HSF also correlated with the extent of histone displacement. The beginning of chromatin remodeling coincides with the polymerase II loading on heat shock gene promoters and is regulated either by HSF binding or activation of preloaded HSF.

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
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