Regulating Chromatin by Histone Acetylation

Steunou, Anne-Lise; Rossetto, Dorine; Côté, Jacques

doi:10.1007/978-1-4614-8624-4_4

Cited by 49 publications

(63 citation statements)

References 448 publications

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“…1C). The Gcn5 HAT is found within different complexes in vivo; namely, ADA/HAT-A2, SAGA, SLIK, and ATAC (Steunou et al 2014). Recombinant yGcn5 enzyme mainly acetylates H3 and, to a lesser extent, H4 in free histones but is unable to target nucleosomes (Kuo et al 1996;Grant et al 1997).…”

Section: Histone Modifier Enzymesmentioning

confidence: 99%

“…Other HATs with less clearly conserved catalytic domains also exist, the most recognized being CBP/p300. Acetyl marks are removed by three major classes of HDACs, classified according to their homology with the yeast enzymes Rpd3, Hda1, and NAD-dependent Sir2/sirtuin (for review, see Steunou et al 2014).…”

mentioning

confidence: 99%

“…In fact, many diseases have been associated with the misincorporation of histone marks. Several other reviews have focused on the mechanisms of PTM misregulation leading to disease (Chi et al 2010;Fullgrabe et al 2011;Smith et al 2011;Dawson and Kouzarides 2012;Shen and Laird 2013;Steunou et al 2014).…”

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confidence: 99%

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Histone target selection within chromatin: an exemplary case of teamwork

2014

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Histone modifiers like acetyltransferases, methyltransferases, and demethylases are critical regulators of most DNA-based nuclear processes, de facto controlling cell cycle progression and cell fate. These enzymes perform very precise post-translational modifications on specific histone residues, which in turn are recognized by different effector modules/proteins. We now have a better understanding of how these enzymes exhibit such specificity. As they often reside in multisubunit complexes, they use associated factors to target their substrates within chromatin structure and select specific histone mark-bearing nucleosomes. In this review, we cover the current understanding of how histone modifiers select their histone targets. We also explain how different experimental approaches can lead to conflicting results about the histone specificity and function of these enzymes.

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Section: Histone Modifier Enzymesmentioning

confidence: 99%

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Histone target selection within chromatin: an exemplary case of teamwork

2014

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Section: Introductionmentioning

confidence: 99%

“…Acetylation of lysine residues also destabilizes the DNA-histone and histone-histone interactions, leading to a more open and dynamic chromatin organization (Steunou et al, 2014). It is catalyzed by lysine acetyltransferases such as the mammalian NuA4/TIP60 complex, a 1.5 MDa multiprotein platform of at least 16 subunits, highly conserved from yeast to human (Steunou et al, 2014). In vivo, TIP60’s major acetylation targets are lysines (K) 5, 8 and 12 on nucleosomal H4, H2AK5, histone variants H2AZ and H2AX, as well as non-histone substrates such as p53 (Steunou et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation

et al. 2016

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SUMMARY The NuA4/TIP60 acetyltransferase complex is a key regulator of genome expression and stability. Here, we identified MBTD1 as a new stable subunit of the complex and gleaned intriguing insights into TIP60’s function. Harboring a histone reader domain for H4K20me1/2, MBTD1 allows TIP60 to associate with specific gene promoters and to promote the repair of DNA double strand breaks by homologous recombination. Interestingly, the non-homologous end joining factor 53BP1 engages chromatin through simultaneous binding of H4K20me2 and H2AK15ub, and it was postulated that Tip60-dependent acetylation of H4 regulates this binding. Our findings now indicate that the TIP60 complex is a potent regulator of DNA damage repair pathways in part by targeting the same histone mark as 53BP1. In addition, deposition of H2AK15ub by RNF168 inhibits chromatin acetylation by TIP60, while this residue can be acetylated by TIP60 in vivo, blocking its ubiquitylation. Altogether, these results uncover an intricate mechanism orchestrated by the TIP60 complex which regulates 53BP1-dependent repair pathway selection through incompatible bivalent binding and modification of chromatin.

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Untersuchung der epigenetischen Funktionen von Lysin‐Acetyltransferasen mit Methoden der chemischen Biologie

Han

Liu

et al. 2017

Angewandte Chemie

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Die Seitenkettenacetylierung von Lysinresten in Histonen und Nicht‐Histon‐Proteinen durch Katalyse mit Lysin‐Acetyltransferasen (KATs) ist eine häufige posttranslationale Modifikation (PTM) in eukaryotischen Zellen. Die Lysin‐Acetylierung spielt eine regulatorische Rolle in wichtigen zellulären Prozessen. Einen besonderen Einfluss hat die KAT‐vermittelte Histon‐Acetylierung für alle durch DNA‐Template vermittelten epigenetischen Vorgänge. In den vergangenen Jahren hat sich gezeigt, dass das Studium von KAT‐Funktionen in biologischen und krankheitsbezogenen Prozessen in großem Maße von exakt konzipierten Strategien der chemischen Biologie profitiert. Hier werden Ansätze der chemischen Biologie zur Untersuchung der KAT‐Aktivität und ‐Funktion erläutert. Diese Methoden und Sonden werden entsprechend ihrem Wirkmechanismus und den jeweiligen Anwendungen eingeteilt, und ihre Stärken und Grenzen werden diskutiert.

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Regulating Chromatin by Histone Acetylation

Cited by 49 publications

References 448 publications

Histone target selection within chromatin: an exemplary case of teamwork

Histone target selection within chromatin: an exemplary case of teamwork

The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation

Untersuchung der epigenetischen Funktionen von Lysin‐Acetyltransferasen mit Methoden der chemischen Biologie

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