Histone acetylation in gene regulation

Verdone, Loredana; Agricola, Eleonora; Caserta, Micaela; Mauro, Ernesto Di

doi:10.1093/bfgp/ell028

Cited by 205 publications

(144 citation statements)

References 153 publications

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“…The ability of histone acetylation to regulate gene expression occurs via the direct effect of this modification on higher order chromatin structure, which serves to neutralize the charge between histone tails and the DNA backbone, and also by serving as a docking site for bromodomaincontaining regulatory factors. In general, hyperacetylation of histones is associated with structurally 'open' chromatin and gene transcription, whereas histone deacetylation is linked to gene repression and/or heterochromatin formation (Verdone et al, 2006). HATs can be divided into three groups on the basis of their catalytic domains and comprise GNATs (Gcn5 N-acetyltransferases) which include Gcn5, p300/CBPassociated factor (PCAF), Elp3, Hat1, Hpa2 and Nut1 members; MYSTs, which include MOZ, MORF, Ybf2/ Sas3, Sas2, HBO1 and Tip60 members; and p300/CBP (cAMP response element-binding (CREB) protein) (Lee and Workman, 2007).…”

Section: Histone Acetyltransferases and Histone Deacetylases: Roles Imentioning

confidence: 99%

Epigenetic regulation of normal and malignant hematopoiesis

2007

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Section: Histone Acetyltransferases and Histone Deacetylases: Roles Imentioning

confidence: 99%

Epigenetic regulation of normal and malignant hematopoiesis

2007

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“…Acetylation and methylation are major post-translational regulators of proteins. Modification of histones (i.e., H3, H4) disrupts the structure of the nucleosome, which leads to DNA relaxation and a subsequent increase in accessibility to transcription factors (14)(15)(16). Mostly, lysine (K) residues of histone proteins are subject to modifications.…”

Section: Introductionmentioning

confidence: 99%

Heparanase expression is associated with histone modifications in glioblastoma

et al. 2011

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Abstract. In this study we investigated epigenetic modifications such as DNA methylation, histone acetylation and histone methylation in the regulation of heparanase expression in glioblastoma. We found that heparanase promoters are differentially methylated among three glioblastoma cell lines; however, all these cells expressed baseline levels of heparanase. 5-Aza-2'-deoxycytidine (5-Aza-dC), a DNA methyltransferase inhibitor, revoked heparanase expression in all the examined cells. Trichostatin A (TSA), a histone deacetylase inhibitor, activated heparanase expression in promoter unmethylated LN229 and T98G cells but not in promoter methylated U251n cells. To identify the mechanisms of heparanase induction by 5-Aza-dC, heparanase expression-related transcription factors were examined. No detected transcription factors (EGR1, Ets1, GABPα and Sp1) were found to be induced either by 5-Aza-dC or TSA. Furthermore, we found that 5-Aza-dC increased acetylation of histone H3 and di-methylation of histone H3 lysine K4 (H3K4me2) in LN229 and T98G cells. The increased histone acetylation and H3K4me2 were also observed in heparanaseexpressing tumor tissues by immunohistochemistry staining. Additionally, we found that nuclear factor κB (NFκB) p65 but not NFκB p50 was correlated with heparanase expression, which could be expressed both by neoplastic cells and angiogenesis-related neovessel cells. However, we did not observe any regulatory mechanism between heparanase and NFκB p65 via transient transfection of their cDNA in T98G and U251n cells. We concluded that heparanase expression is associated with histone modifications and promoter DNA methylation plays a role in the control of gene silencing. Overexpression of both heparanase and NFκB p65 may be the result of excessive histone modifications.

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“…9,13 This is because of the high force sensitivity of AFM cantilevers and the relatively high strength of electrostatic forces at nm distances. Employing KFM to detect and follow subtle charge alterations on surfaces could open up entirely new routes for functional imaging, especially in biophysics, a few examples being enzymatic reactions, 30 glycation, 28 histone-DNA interactions, 31 or the influence of charged peptides on membranes. 32 The authors would like to thank the Engineering and Physical Sciences Research Council (EPSRC) for funding of this project through a DTG studentship (Grant Ref.…”

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confidence: 99%

Kelvin-probe force microscopy of the pH-dependent charge of functional groups

Stone

Mesquida

2016

Applied Physics Letters

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Kelvin-probe Force Microscopy (KFM) is an established method to map surface potentials or surface charges at high, spatial resolution. However, KFM does not work in water, which restricts its applicability considerably, especially when considering common, functional chemical groups in biophysics such as amine or carboxy groups, whose charge depends on pH. Here, we demonstrate that the KFM signal of such groups taken in air after exposure to water correlates qualitatively with their expected charge in water for a wide range of pH values. The correlation was tested with microcontact-printed thiols exposing amine and carboxy groups. Furthermore, it was shown that collagen fibrils, as an example of a biological material, exhibit a particular, pH-sensitive surface charge pattern, which could be caused by the particular arrangement of ionizable residues on the collagen fibril surface.

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Histone acetylation in gene regulation

Cited by 205 publications

References 153 publications

Epigenetic regulation of normal and malignant hematopoiesis

Epigenetic regulation of normal and malignant hematopoiesis

Heparanase expression is associated with histone modifications in glioblastoma

Kelvin-probe force microscopy of the pH-dependent charge of functional groups

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