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Genome-Wide Replication-Independent Histone H3 Exchange Occurs Predominantly at Promoters and Implicates H3 K56 Acetylation and Asf1
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In yeast, histone H3/H4 exchange independent of replication is poorly understood. Here, we analyzed the deposition of histone H3 molecules, synthesized during G1, using a high-density microarray histone exchange assay. While we found that H3 exchange in coding regions requires high levels of transcription, promoters exchange H3 molecules in the absence of transcription. In inactive promoters, H3 is deposited predominantly in well-positioned nucleosomes surrounding nucleosome-free regions, indicating that some nucleosomes in promoters are dynamic. This could facilitate induction of repressed genes. Importantly, we show that histone H3 K56 acetylation, a replication-associated mark, is also present in replication-independent newly assembled nucleosomes and correlates perfectly with the deposition of new H3. Finally, we found that transcription-dependent incorporation of H3 at promoters is highly dependent on Asf1. Taken together, our data underline the dynamic nature of replication-independent nucleosome assembly/disassembly, specify a link to transcription, and implicate Asf1 and H3 K56 acetylation.
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“Histone chaperones and ATP-dependent chromatin-remodelling complexes are accordingly important for gene regulation given they regulate nucleosome dynamics at promoters, restricting or increasing promoter accessibility for recruitment of transcription factors and RNA polymerase II (Pol II)19–23.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [21]
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Cites
Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast
Pokholok, D., Harbison, C. T., Levine, S. S., Cole, M. F., Hannett, N. M., Lee, T. I., Bell, G. W., Walker, K., Rolfe, A., Herbolsheimer, E., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.026 · Cited by 1,477
Genome-Scale Identification of Nucleosome Positions in S. cerevisiae
Yuan, G., Liu, Y.-J., Dion, M. F., Slack, M. D., Wu, L. F., Altschuler, S. J., & Rando, O. J. (2005) · Science · doi:10.1126/science.1112178 · Cited by 1,139
From Silencing to Gene Expression
Janicki, S. M., Tsukamoto, T., Salghetti, S. E., Tansey, W. P., Sachidanandam, R., Prasanth, K. V., Ried, T., Shav-Tal, Y., Bertrand, E., Singer, R. H., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00171-0 · Cited by 704
Histone Variant H2A.Z Marks the 5′ Ends of Both Active and Inactive Genes in Euchromatin
Raisner, R. M., Hartley, P. D., Meneghini, M. D., Bao, M. Z., Liu, C. L., Schreiber, S. L., Rando, O. J., & Madhani, H. D. (2005) · Cell · doi:10.1016/j.cell.2005.10.002 · Cited by 676
Dynamics of Replication-Independent Histone Turnover in Budding Yeast
Dion, M. F., Kaplan, T., Kim, M., Buratowski, S., Friedman, N., & Rando, O. J. (2007) · Science · doi:10.1126/science.1134053 · Cited by 556
Zhang, H., Roberts, D. N., & Cairns, B. R. (2005) · Cell · doi:10.1016/j.cell.2005.08.036 · Cited by 545
A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Masumoto, H., Hawke, D., Kobayashi, R., & Verreault, A. (2005) · Nature · doi:10.1038/nature03714 · Cited by 544
Genome-scale profiling of histone H3.3 replacement patterns
Mito, Y., Henikoff, J. G., & Henikoff, S. (2005) · Nature Genetics · doi:10.1038/ng1637 · Cited by 526
Guillemette, B., Bataille, A. R., Gévry, N. Y., Adam, M., Blanchette, M., Robert, F., & Gaudreau, L. R. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030384 · Cited by 454
Self-citationYeast Rtt109 Promotes Genome Stability by Acetylating Histone H3 on Lysine 56
Driscoll, R., Hudson, A., & Jackson, S. P. (2007) · Science · doi:10.1126/science.1135862 · Cited by 439
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Radman‐Livaja, M., Quan, T. K., Valenzuela, L., Armstrong, J. A., van Welsem, T., Kim, T. S., Lee, L. J., Buratowski, S., van Leeuwen, F., Rando, O. J., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002811 · Cited by 66
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Wang, A. Y., Schulze-Hentrich, J. M., Skordalakes, E., Gin, J. W., Berger, J. M., Rine, J., & Kobor, M. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906539106 · Cited by 66
Korber, P., & Barbarić, S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku784 · Cited by 65
Sitbon, D., Boyarchuk, E., Dingli, F., Loew, D., & Almouzni, G. (2020) · Nature Communications · doi:10.1038/s41467-020-15084-4 · Cited by 71
Thebault, P., Boutin, G., Bhat, W. W., Rufiange, A., Martens, J. A., & Nourani, A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01083-10 · Cited by 64
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Klopf, E., Pašková, Ľ., Solé, C., Martín, G. M., Petryshyn, A., Posas, F., Wintersberger, U., Ammerer, G., & Schüller, C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01858-08 · Cited by 65
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Rossetto, D., Cramet, M., Wang, A. Y., Steunou, A., Lacoste, N., Schulze-Hentrich, J. M., Côté, V., Saksouk, J., Piquet, S., Nourani, A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201386433 · Cited by 57
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Metadata
- Authors
- Rufiange, A., Jacques, P.-É., Bhat, W., Robert, F., & Nourani, A.
- Affiliations
- Centre hospitalier universitaire de Québec (CA)
- Montreal Clinical Research Institute (CA)
- Corresponding author
- Nourani, Amine
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 27
- Issue
- 3
- Pages
- 393-405
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1980716967
- Cited by
- 313
- References
- 28
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 7 · 2023: 14 · 2022: 5 · 2021: 14 · 2020: 20 · 2019: 10 · 2018: 10 · 2017: 8 · 2016: 12 · 2015: 23 · 2014: 26 · 2013: 26 · 2012: 28
- FWCI
- 9.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- promoter, Asf1, nucleosome assembly, nucleosome dynamics, nucleosome-free regions, transcription, gene repression, Saccharomyces cerevisiae
- MeSH terms
- Acetylation, Chromatin, Cytosol, DNA Replication, HeLa Cells, Histones, Humans, Promoter Regions, Genetic, Protein Processing, Post-Translational, Saccharomyces cerevisiae, S Phase, Genome, Fungal, Cell Cycle Proteins, Molecular Chaperones, Saccharomyces cerevisiae Proteins, Chromatin Immunoprecipitation, Immunoprecipitation
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