The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure

Mersfelder, Erica L.; Parthun, Mark R.

doi:10.1093/nar/gkl338

Cited by 182 publications

(153 citation statements)

References 107 publications

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“…15,16 This list is very likely to be growing in the near future given that mass spectrometry approaches have identified numerous novel histone modifications, whose roles are still to be determined. 18 While some modifications like H2AX phosphorylation (gH2AX) are induced by DNA damage, 19 others are normally cell-cycle regulated but persist after damage, as recently shown for H3K56 acetylation in yeast. 20 Finally, constitutive modifications can also provide specific binding sites for DNA damage response proteins, as described for methylation of H4K20 in fission yeast, 21 H3K79 in budding yeast 22,23 and both H3K79 and H4K20 in higher eukaryotes, 24,25 where determination of the relevant methylation site is still a matter of debate.…”

Section: Chromatin Rearrangements Crosstalk With the Dna Damage Responsementioning

confidence: 93%

DNA Damage Leaves its Mark on Chromatin

Polo¹,

Almouzni²

2007

Cell Cycle

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DNA organization into chromatin has a major influence on the cellular response to DNA damage. Recent studies in various systems ranging from yeast to human cells stress the importance of chromatin not simply as a barrier to DNA repair processes but also as an active contributor to the DNA damage response. Indeed, modulations of chromatin organization involving various degrees of rearrangements, such as histone modifications and even nucleosome displacement, can promote efficient repair and also participate in checkpoint signaling. Here, we survey recent progress in delineating how chromatin rearrangements provide crosstalk with the DNA damage response. In particular, we highlight new data on histone dynamics at damage sites and discuss their functional importance for the stable propagation of specific chromatin states.

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Section: Chromatin Rearrangements Crosstalk With the Dna Damage Responsementioning

confidence: 93%

DNA Damage Leaves its Mark on Chromatin

Polo¹,

Almouzni²

2007

Cell Cycle

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“…Based on this interpretation, the biotin attachment sites were located predominantly in the N-terminal tail, specifically at lysines 5, 9, 13, or 15. Lysine 36, a residue within the globular domain of H2A on the lateral surface of the protein, 24 was also found to be biotinylated in the first hour of incubation. Interestingly, a lysine from the linker region connecting the His-tag to the native protein (labeled as position À5 in Table I) also showed a biotin attachment.…”

Section: Localization Of Nonenzymatic Biotin Attachment Sitesmentioning

confidence: 98%

Nonenzymatic biotinylation of histone H2A

et al. 2009

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Holocarboxylase synthetase (HCS, eukaryotic enzyme) and BirA (prokaryotic) are biotin protein ligases that catalyze the ATP-dependent attachment of biotin to apocarboxylases via the reactive intermediate, bio-5 0 -AMP. In this study, we examined the in vitro mechanism of biotin attachment to histone H2A in the presence of HCS and BirA. The experiment derives from our observations that HCS is found in the nucleus of cells in addition to the cytoplasm, and it has the ability to attach biotin to histones in vitro (Narang et al., Hum Mol Genet 2004; 13:15-23). Using recombinant HCS or BirA, the rate of biotin attachment was considerably slower with histone H2A than with the biotin binding domain of an apocarboxylase. However, on incubation of recombinant H2A with chemically synthesized bio-5 0 -AMP, H2A was observed to be rapidly labeled with biotin in the absence of enzyme. Nonenzymatic biotinylation of a truncated apocarboxylase (BCCP87) has been previously reported (Streaker and Beckett, Protein Sci 2006; 15:1928-1935), though at a much slower rate than we observe for H2A. The specific attachment sites of nonenzymatically biotinylated recombinant H2A at different time points were identified using mass spectrometry, and were found to consist of a similar pattern of biotin attachment as seen in the presence of HCS, with preference for lysines in the highly basic N-terminal region of the histone. None of the lysine sites within H2A resembles the biotin attachment consensus sequence seen in carboxylases, suggesting a novel mechanism for histone biotinylation.

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“…This has led to the discovery of a myriad of novel histone modifications, many of which have yet to be ascribed a biological function. 1,2 Six independent research groups recently reported the discovery of lysine 56 as a novel site of histone H3 acetylation in the budding yeast Saccharomyces cerevisiae. [3][4][5][6][7][8] K56 acetylation has also been observed in the fission yeast Schizosaccharomyces pombe, 6 which is evolutionarily very distant from S. cerevisiae.…”

Section: Introductionmentioning

confidence: 99%

Histone H3 Lysine 56 Acetylation: A New Twist in the Chromosome Cycle

Özdemir¹,

Masumoto²,

Fitzjohn³

et al. 2006

Cell Cycle

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Several recent reports have identified lysine 56 (K56) as a novel site of acetylation in yeast histone H3. K56 acetylation is predicted to disrupt some of the histone-DNA interactions at the entry and exit points of the nucleosome core particle. This modification occurs in virtually all the newly synthesised histones that are deposited into chromatin during S-phase. Cells with mutations that block K56 acetylation show increased genome instability and hypersensitivity to genotoxic agents that interfere with replication. Removal of K56 acetylation takes place in the G 2 /M phase of the cell cycle and is dependent upon Hst3 and Hst4, two proteins that are related to the NAD + -dependent histone deacetylase Sir2. In response to DNA damage checkpoint activation during S-phase, expression of Hst3/Hst4 is delayed to extend the window of opportunity in which K56 acetylation can act in the DNA damage response. The high abundance of histone H3 K56 acetylation, its regulation and strategic location in the nucleosome core particle raise a number of fascinating issues that we discuss here.

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The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure

Cited by 182 publications

References 107 publications

DNA Damage Leaves its Mark on Chromatin

DNA Damage Leaves its Mark on Chromatin

Nonenzymatic biotinylation of histone H2A

Histone H3 Lysine 56 Acetylation: A New Twist in the Chromosome Cycle

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