Transcription histone acetylation

Agalioti T, Chen G, Thanos D (2002) Deciphering the transcriptional histone acetylation code for a human gene. Cell 111 381-392... 

Histone acetylation is a hallmark of open and accessible chromatin structure, which results in activation of gene transcription. Histone acetylation leads to the recruitment of a number of bromodomain-containing proteins (BRDs) that exclusively recognize e-Af-acetylated lysine residues. These specific protein interaction modules, also called epigenetic reader domains, are evolutionarily highly conserved. The human proteome encodes 61 bromodomain interaction domains present in 42 proteins comprising chromatin modifying enzymes (histone... 

More subtle modes of action are also possible since the response to hormone receptor binding is complex and could be affected by chemical interference with receptor-related proteins, DNA methylation or histone acetylation. Dioxin (TCDD), for example, reduces the ability of the oestrogen-receptor complex to bind to the oestrogen response element of DNA, reducing gene transcription. ... 

Clock gene and transcription factor with histone acetyl-transferase (HAT) activity that (in complex with BMAL1) constitutes a positive limb of molecular circadian oscillators. 

Cytokines such as TNFa and IL-1 3, acting via NF-kB, can induce histone acetylation in both a time- and concentration-dependent manner. Upon DNA binding, NF-kB recruits transcriptional coactivators such as CREB binding protein (CBP) and p300/CBP-associated factor (PCAF). 

Clayton AL, Hazzalin CA, Mahadevan LC (2006) Enhanced histone acetylation and transcription a dynamic perspective. Mol Cell 23 289-96... 

A model called histone code theory includes more aspects of chromatin regulation which have been identified. The histone code theory predicts that histone acetylation and other posttranslational histone modifications serve as binding sites for regulatory proteins which mediate processes like gene transcription upon recruitment (see Fig. 2b) [3]. In this context histone modifications can be understood as... 

Beside coactivators so-called corepressors exist that are bound to transcription factors such as nuclear receptors and inhibit the initiation of transcription. These factors include the nuclear receptor corepressor (NCoR) and the silencing mediator of retinoic acid and thyroid hormone receptor (SMRT), which interact with nuclear receptors and serve as platforms for complexes containing histone deacetylases (HDACs). These enzymes cause the reversal of histone acetylation of histones leading to a tightening of chromatin and enhancing its inaccessibility for RNA polymerase containing complexes. 

Grunstein M Histone acetylation in chromatin structure and transcription. Nature 1997 389 349. 

JDP2 H2A-H2B H3-H4 Regulates transcription via inhibition of p300 mediated histone acetylation... 

Kurten S, Obe, G (1975) Premature chromosome condensation in the bone marrow of Chinese hamster after pUcation of bleomycin in vivo. Mutat Res 27(2) 285—294 Lee DY, Hayes JJ, Pruss D, Wolffe AP (1993) A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 72 73—84... 

Figure 4. Therapeutic strategies to counteract CBP loss of function. CBP loss of function leads to a decrease in histone acetylation levels as well as a decrease in CBP-dependent transcription. Two main approaches can be tested to reverse diis process either resetting HAT functionality or resetting global acetylation levels widi die use of HDAC inhibitors. Whereas both strategies would increase histone acetylation levels, HDAC inhibition would act on a broad range of genes, while CBP activation (overexpression or by a pharmacological approach) would specifically target bodi CBP-dependent histone acetylation and transcription. The structure of some of the HDACi that have been tested in different models, such as small fatty acids and hydroxamic acids, are represented in the boxes...

Utley RT, Lacoste N, Jobin-Robitaille O, Allard S, Cote J (2005) Regulation of NuA4 histone acetyl-transferase activity in transcription and DNA repair by phosphorylation of histone H4. Mol Cell Biol 25(18) 8179-8190... 

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