Effects of histone acetylation on chromatin structure

Gavazzo, Paola; Vergani, Laura; Mascetti, G; Nicolini, Claudio

doi:10.1002/(sici)1097-4644(19970301)64:3<466::aid-jcb13>3.0.co;2-e

Cited by 17 publications

(11 citation statements)

References 26 publications

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“…Some modifications such as acetylation of lysine residues in histones H3 upregulate transcription while other modifications like methylation of H3K9 downregulate transcription [15, 16]. Among all the modifications, histone acetylation happens most frequently [17]. Histone acetylation is catalyzed by histone acetyltransferases (HATs) that transfer acetyl groups from acetyl coenzyme A (acetyl-CoA) onto the ε -amino groups of conserved lysine residues within the core histones.…”

Section: Introductionmentioning

confidence: 99%

Effects of In Vitro Maturation on Histone Acetylation in Metaphase II Oocytes and Early Cleavage Embryos

Wang

Fang

Zhan

et al. 2010

Obstetrics and Gynecology International

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In vitro maturation (IVM) of oocyte is an effective procedure for avoiding ovarian hyperstimulation syndrome in patients with polycystic ovaries (PCOS) during in vitro fertilization (IVF). To investigate the influences of IVM on epigenetic reprogramming and to search for the possible reasons for the lower rates of fertilization and cleavage in IVM oocytes, we examined the expression of two enzymes controlling histone acetylation, histone acetyltransferase GCN5 (GCN5) and histone deacetylase 1 (HDAC1), as well as their common target, acetyl-histone H3 (Ac-H3), in mouse metaphase II (MII) oocytes and preimplantation embryos. Results showed that IVM downregulated the protein expression of GCN5 in MII oocytes and two-cell embryos and changed the distribution of GCN5 in two-cell embryos. Expression of HDAC1 mRNA in MII oocytes and two-cell embryos decreased in the IVM group. However, none of these changes persisted after two-cell embryos. Levels of Ac-H3 in both oocytes and embryos remained unchanged after IVM. Our studies indicated that IVM could affect the protein and gene expression related to histone acetylation in oocytes and early cleavage embryos. By function of selection, parts of the changes could be recovered in late embryo development.

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Section: Introductionmentioning

confidence: 99%

Effects of In Vitro Maturation on Histone Acetylation in Metaphase II Oocytes and Early Cleavage Embryos

Wang

Fang

Zhan

et al. 2010

Obstetrics and Gynecology International

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“…The different effects of histone acetylaion on chromatin organization have been analyzed both in vitro and in vivo [10,11] and in mitosis and in meiosis [12]. Recent results show that the acetylation of different lysines of histone is associated with a diversity of chromatin-related processes in mitosis [13] and is necessary for orderly meiosis [6].…”

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confidence: 99%

Dynamic Changes in Histone Acetylation During Sheep Oocyte Maturation

Tang

Wang

Xiong

et al. 2007

Journal of Reproduction and Development

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Abstract. The changes in histone acetylation are not always consistent in various cell types and at different developmental stages. We immunostained specific antibodies against acetylated lysine 9 of histone H3 and acetylated lysines 5 and 12 of histone H4 in an effort to understand the detailed changes in histone acetylation during sheep oocyte meiosis. We found that the acetylation fluorescence signals of H3/K9 and H4/K12 on chromatin appeared intensively in the germinal vesicle (GV), late-GV (L-GV), and germinal vesicle breakdown (GVBD) stages and became weak in metaphase I (MI); however staining reappeared in anaphase I-telophase-I (AI-TI) and metaphase II (MII). Furthermore, staining was detected in the first polar bodies. The fluorescence signals of H4/K5 first appeared in the MI stage and became intensive in the AI-TI stage; however they were barely detectable in MII stage chromosomes and first polar bodies. We conclude that the acetylation patterns of H3/K9 and H4/K12 during oocyte meiotic maturation are similar and that the pattern of H4/K5 is unique. Key words: Histone acetylation, Meiotic maturation, Sheep oocyte, Trichostain A (J. Reprod. Dev. 53: [555][556][557][558][559][560][561] 2007) h e b a s i c s t r u c t u r a l u n i t o f e u k a r y o t i c chromosomes is a DNA protein complex called the nucleosome that consists of 147 base pairs of DNA wrapped around an octamer of the H2A, H2B, H3, and H4 histone proteins. The nucleosome histones are thought to play important roles in various cellular functions. It is well known that post-translational acetylation, methylation, phosphorylation, and ubiquitination of histones play an intrinsic role in transcription regulation [1,2]. In these post-translational modifications, h i s t o n e a c e t y l a t i o n a f f e c t s c h r o m a t i o n conformation [3], correlates with gene activity [4,5], and is required for orderly meiosis [6]. The Nterminal tails of histone H3 and H4 have a critical role in the folding of higher order chromatin structure [7][8][9]. The different effects of histone acetylaion on chromatin organization have been analyzed both in vitro and in vivo [10,11] and in mitosis and in meiosis [12]. Recent results show that the acetylation of different lysines of histone is associated with a diversity of chromatin-related processes in mitosis [13] and is necessary for orderly meiosis [6]. The lysine residue-specific changes in histone acetylation during pig oocyte meiosis have distinctive characteristics [6,15] compared with those of mouse oocytes [14].In the present study, we investigated the changes in acetylation of lysine K9 of histone H3, and lysine K5, K12 of histone H4 in sheep oocytes at different stages of maturation.

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“…It has long been thought that because acetylation neutralizes the positive charge on the histones, this modification facilitates the open configuration of the chromatin at actively expressed regions in the chromatin (85,86). Indeed, hypoacetylation is found at promoter sites of genes with low or no expression levels, whereas acetylated histone tails are mainly associated with active genes (84,87).…”

Section: Gene Expression Modulation With Targeted Epigenetic Editorsmentioning

confidence: 99%

Epigenetic Editing: targeted rewriting of epigenetic marks to modulate expression of selected target genes

Groote

Verschure

Rots

2012

Nucleic Acids Research

154

115

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Despite significant advances made in epigenetic research in recent decades, many questions remain unresolved, especially concerning cause and consequence of epigenetic marks with respect to gene expression modulation (GEM). Technologies allowing the targeting of epigenetic enzymes to predetermined DNA sequences are uniquely suited to answer such questions and could provide potent (bio)medical tools. Toward the goal of gene-specific GEM by overwriting epigenetic marks (Epigenetic Editing, EGE), instructive epigenetic marks need to be identified and their writers/erasers should then be fused to gene-specific DNA binding domains. The appropriate epigenetic mark(s) to change in order to efficiently modulate gene expression might have to be validated for any given chromatin context and should be (mitotically) stable. Various insights in such issues have been obtained by sequence-specific targeting of epigenetic enzymes, as is presented in this review. Features of such studies provide critical aspects for further improving EGE. An example of this is the direct effect of the edited mark versus the indirect effect of recruited secondary proteins by targeting epigenetic enzymes (or their domains). Proof-of-concept of expression modulation of an endogenous target gene is emerging from the few EGE studies reported. Apart from its promise in correcting disease-associated epi-mutations, EGE represents a powerful tool to address fundamental epigenetic questions.

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Effects of histone acetylation on chromatin structure

Cited by 17 publications

References 26 publications

Effects of In Vitro Maturation on Histone Acetylation in Metaphase II Oocytes and Early Cleavage Embryos

Effects of In Vitro Maturation on Histone Acetylation in Metaphase II Oocytes and Early Cleavage Embryos

Dynamic Changes in Histone Acetylation During Sheep Oocyte Maturation

Epigenetic Editing: targeted rewriting of epigenetic marks to modulate expression of selected target genes

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