Role of Histone Acetylation in the Assembly and Modulation of Chromatin Structures

Annunziato, Anthony T.; Hansen, Jeffrey C.

doi:10.3727/000000001783992687

Cited by 142 publications

(111 citation statements)

References 219 publications

(60 reference statements)

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“…The covalent addition of an acetyl group to the e-amino group of a lysine residue has been postulated to affect chromatin at two levels. First, acetylation impacts chromatin structure through the neutralization of the charge inherent to the amino group of lysine, thereby weakening intra-and inter-nucleosomal interactions of the chromatin fiber and facilitating its decondensation by increasing accessibility to the nucleosomal DNA (Annunziato and Hansen, 2000;Kouzarides, 2000). Second, acetylation is recognized/targeted by specific factors such as transcription regulators or ATP-dependent remodeling activities.…”

Section: Acetylation Of Histonesmentioning

confidence: 99%

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

2007

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Histone deacetylases (HDACs) catalyse the removal of acetyl groups from the N-terminal tails of histones. All known HDACs can be categorized into one of four classes (I-IV). The class III HDAC or silencing information regulator 2 (Sir2) family exhibits characteristics consistent with a distinctive role in regulation of chromatin structure. Accumulating data suggest that these deacetylases acquired new roles as genomic complexity increased, including deacetylation of non-histone proteins and functional diversification in mammals. However, the intrinsic regulation of chromatin structure in species as diverse as yeast and humans, underscores the pressure to conserve core functions of class III HDACs, which are also known as Sirtuins. One of the key factors that might have contributed to this preservation is the intimate relationship between some members of this group of proteins (SirT1, SirT2 and SirT3) and deacetylation of a specific residue in histone H4, lysine 16 (H4K16). Evidence accumulated over the years has uncovered a unique role for H4K16 in chromatin structure throughout eukaryotes. Here, we review the recent findings about the functional relationship between H4K16 and the Sir2 class of deacetylases and how that relationship might impact aging and diseases including cancer and diabetes.

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Section: Acetylation Of Histonesmentioning

confidence: 99%

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

2007

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“…Each of these modifications alters chromatin structure through effects on histone: DNA, histone:histone, and nucleosome:nucleosome interactions (Ura et al, 1997;Annunziato and Hansen, 2000). In addition, histone modifications affect the binding of nonhistone proteins to chromatin, including transcription factors and additional chromatin remodeling activities (Winston and Allis, 1999;Jenuwein and Allis, 2001;Kim et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Developmental potential of Gcn5^−/− embryonic stem cells in vivo and in vitro

Lin

Srajer

Evrard

et al. 2007

Developmental Dynamics

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Gcn5 is a prototypical histone acetyltransferase (HAT) that serves as a coactivator for multiple DNA-bound transcription factors. We previously determined that deletion of Gcn512 (hereafter referred to as Gcn5) causes embryonic lethality in mice. Gcn5 null embryos undergo gastrulation but exhibit high levels of apoptosis, leading to loss of mesodermal lineages. To further define the functions of Gcn5 during development, we created Gcn5 ؊/؊ mouse embryonic stem (ES) cells. These cells survived in vitro and formed embryoid bodies (EBs) that expressed markers for ectodermal, mesodermal, and endodermal lineages.

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“…Lysines on the N-terminal tails of histones (H4: K5, K8, K12 and K16; H3: K9, K14, K18 and K23) are subject to acetylation [21]. Acetylation of histones occurs at the ε-amine group of a lysine residue, removing positive charges and thus reducing the electrostatic affinity of histones to the negatively charged DNA.…”

mentioning

confidence: 99%

Mass spectrometry-based strategies for characterization of histones and their post-translational modifications

Ren

Freitas

2007

Expert Review of Proteomics

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Due to the intimate interactions between histones and DNA, the characterization of histones has become the focus of great attention. A series of mass spectrometry-based technologies have been dedicated to the characterization and quantitation of different histone forms. This review focuses on the discussion of mass spectrometry-based strategies used for the characterization of histones and their post-translational modifications. Keywordshistone; mass spectrometry; post-translational modification Histones are a group of highly conserved proteins throughout eukaryotic evolution [1]. The core histones (H4, H3, H2A and H2B) form an octamer, in which a H2A-H2B dimer associates on each side of the H3-H4 tetramer through an interaction between the C-terminal halves of H2B and H4 [2]. The negatively charged DNA superhelix wraps around the histone octamer to form repeating nucleosome cores, which further assemble into higher order chromatin fibers stabilized by the linker histones (H1 and H5) and linker DNA [3]. The histone fold regions in core histones are highly conserved α-helices, which are connected by two loops. The third histone structural motif comprises the flexible and irregular histone tails, which are extended and reach outside of the nucleosomal unit to interact with DNA [4]. Challenge of molecular characterization: post-translational modifications & sequence variationsAs a building block of the nucleosome, histones play an important role in chromatin assembly and affect the interactions between DNA and other chromatin-associated proteins. Histones regulate gene transcription through their diverse post-translational modifications (PTMs), which include lysine acetylation, lysine and arginine methylation, serine and threonine phosphorylation, lysine ubiquitination, lysine sumoylation, and poly-ADP-ribosylation of glutamic acid [5][6][7][8]. Among all the PTMs, histone acetylation and methylation have been most †

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Role of Histone Acetylation in the Assembly and Modulation of Chromatin Structures

Cited by 142 publications

References 219 publications

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

Developmental potential of Gcn5^−/− embryonic stem cells in vivo and in vitro

Mass spectrometry-based strategies for characterization of histones and their post-translational modifications

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Role of Histone Acetylation in the Assembly and Modulation of Chromatin Structures

Cited by 142 publications

References 219 publications

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

Developmental potential of Gcn5−/− embryonic stem cells in vivo and in vitro

Mass spectrometry-based strategies for characterization of histones and their post-translational modifications

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Product

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About

Developmental potential of Gcn5^−/− embryonic stem cells in vivo and in vitro