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Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
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Chromatin assembly factor 1 (CAF-1) and Rtt106 participate in the deposition of newly synthesized histones onto replicating DNA to form nucleosomes. This process is critical for the maintenance of genome stability and inheritance of functionally specialized chromatin structures in proliferating cells. However, the molecular functions of the acetylation of newly synthesized histones in this DNA replication-coupled nucleosome assembly pathway remain enigmatic. Here we show that histone H3 acetylated at lysine 56 (H3K56Ac) is incorporated onto replicating DNA and, by increasing the binding affinity of CAF-1 and Rtt106 for histone H3, H3K56Ac enhances the ability of these histone chaperones to assemble DNA into nucleosomes. Genetic analysis indicates that H3K56Ac acts in a nonredundant manner with the acetylation of the N-terminal residues of H3 and H4 in nucleosome assembly. These results reveal a mechanism by which H3K56Ac regulates replication-coupled nucleosome assembly mediated by CAF-1 and Rtt106.
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“Rtt106, a fungal-specific histone chaperone, functions in histone deposition during DNA replication and transcription elongation in S. cerevisiae, and preferentially binds H3K56-acetylated histone H3-H424–26.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [25]
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The Tango of Histone Marks and Chaperones at Replication Fork
Falbo, K. B., & Shen, X. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.019
“Other acetylation marks on histone H3 at K9, K14, K18, K23, and K27 have also been implicated in nucleosome assembly (Li et al., 2008).”
BackgroundA study of chromatin dynamics during transcription by fluorescence light microscopy
Dickerson, D. R. (2010) · OpenGrey (Institut de l'Information Scientifique et Technique)
Turner, E. L. (2011) · University Library - University of Saskatchewan (University of Saskatchewan)
da Rosa, J. L. (2012) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/w35r-7869
“replication-dependent histone chaperones CAF-1 (chromatin assembly factor 1) and Rtt106 (Li et al., 2008; Su et al., 2012; Zunder et al., 2012).”
InfluentialCharacterisation of the (H3-H4)2-tetramer and its interaction with histone chaperones
Bowman, A. J. (2010) · Discovery Research Portal (University of Dundee)
Dynamics of H4 K16 acetylation by the SAS-I complex in Saccharomyces cerevisiae
Reiter, C. G. (2014) · doi:10.18452/17041
“In contrast to H3 K9Ac and acetylation of H4, Asf1-Rtt109-mediated H3 K56Ac was shown to strongly enhance the affinity of CAF-1 as well as Rtt106 for H3 and to promote the incorporation of new histones into nucleosomes (Li et al. 2008).”
BackgroundProgeria and Genome Instability
Meng, F., Liu, B., & Zhou, Z. (2015) · Springer eBooks · doi:10.1007/978-4-431-55763-0_3
Méndez, J. (2010) · Cell Cycle · doi:10.4161/cc.9.24.14060
Groth, A., & Almouzni, G. (2009) · Royal Society of Chemistry eBooks · doi:10.1039/9781847559852-00297
Regulation of Chromatin by FACT and NuA3
Chruscicki, A. (2014) · cIRcle (University of British Columbia) · doi:10.14288/1.0073776
The Role of ADA3 Overexpression in Proliferation Through Enhancing MYC Expression
Griffin, N. I. (2016) · DigitalCommons@UNMC
A two-colour reporter screen and application to cell cycle transcription.
Kainth, P. (2010) · TSpace (University of Toronto)
The interaction between Rad9 and Tousled-like kinase 1 in the cell cycle and the DNA damage response
Kelly, R. M. (2013) · QSpace (Queen's University Library)
Control of histone variant H3.3 loading on chromatin
Ivanauskiene, K. (2016) · NORA - Norwegian Open Research Archives
HDACi-induced DNA damage: identifying potential endpoints for safety assessment
Wang, W. (2016) · ORCA Online Research @Cardiff (Cardiff University)
Chromatin Remodeling During Homologous Recombination Repair in Saccharomyces Cerevisiae
Osley, M. A. (2014) · Springer eBooks · doi:10.1007/978-1-4614-6436-5_77-2
Kochan, D. Z., Mawer, J. S. P., Tishinov, K., Parekh, S., Massen, J., Graef, M., Spang, A., & Tessarz, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.13.249912
Targeting (de)acetylation: A Diversity of Mechanism and Disease
Quaas, C. E., & Long, D. T. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00076-1
Dissecting the DNA damage-induced transcription stress response
Geijer, M. E. (2021) · RePub (Erasmus University Rotterdam)
ASF1 activation PI3K/AKT pathway regulates sexual and asexual development in filamentous ascomycetePreprint
Wang, S., Liu, X., Xiong, C., Gao, S., Xu, W., Zhao, L., Song, C., Li, Z., & Zhang, X.-G. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.18.464864
“…normal cell cycle progression (Groth et al., 2007, Sutton et al., 2001), genomic instability along with histone modification (Das et al., 2014; Li et al., 2008; Recht et al., 2006; Yuan et al., 2009), DNA replication, repair, recombination and transcriptional regulation (Mousson et al., 2007).”
BackgroundRole of Histone Metabolism and Chromatin Structure in DNA Repair
Kari, V. (2014) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4552
Histone Chaperones, Epigenetics, and Cancer
Rafiei, M., & Bremner, R. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7931-4_15
Metadata
- Authors
- Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z.
- Affiliations
- Mayo Clinic (US)
- Institute for Research in Immunology and Cancer (CA)
- Corresponding author
- Verreault, Alain
- Zhang, Zhiguo
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 134
- Issue
- 2
- Pages
- 244-255
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2597342
- OpenAlex
- W1965975821
- Cited by
- 447
- References
- 47
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 12 · 2023: 20 · 2022: 15 · 2021: 23 · 2020: 14 · 2019: 16 · 2018: 20 · 2017: 22 · 2016: 35 · 2015: 22 · 2014: 34 · 2013: 32 · 2012: 35
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1842 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM072719, R01GM081838)
- 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 › Epigenetics and DNA Methylation
- Keywords
- histone H3 lysine 56 acetylation, CAF-1, histone chaperone, histone deposition, genome stability, histone acetylation, chromatin inheritance
- MeSH terms
- Acetylation, DNA Damage, DNA Replication, DNA, Fungal, Histones, Humans, Lysine, Mutation, Nucleosomes, Ribonucleases, Saccharomyces cerevisiae, S Phase, Protein Structure, Tertiary, Molecular Chaperones, Saccharomyces cerevisiae Proteins
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