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Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Open accessAbstract
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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“In yeast, a recent study reported that H3K56ac plays an important part in nucleosome assembly by increasing the affinity of the chromatin assembly factor 1 (Caf1) chaperone for H3 (Ref”
Background
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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