Epigenetic control of rDNA loci in response to intracellular energy status
Open accessAbstract
Intracellular energy balance is important for cell survival. In eukaryotic cells, the most energy-consuming process is ribosome biosynthesis, which adapts to changes in intracellular energy status. However, the mechanism that links energy status and ribosome biosynthesis is largely unknown. Here, we describe eNoSC, a protein complex that senses energy status and controls rRNA transcription. eNoSC contains Nucleomethylin, which binds histone H3 dimethylated Lys9 in the rDNA locus, in a complex with SIRT1 and SUV39H1. Both SIRT1 and SUV39H1 are required for energy-dependent transcriptional repression, suggesting that a change in the NAD(+)/NADH ratio induced by reduction of energy status could activate SIRT1, leading to deacetylation of histone H3 and dimethylation at Lys9 by SUV39H1, thus establishing silent chromatin in the rDNA locus. Furthermore, eNoSC promotes restoration of energy balance by limiting rRNA transcription, thus protecting cells from energy deprivation-dependent apoptosis. These findings provide key insight into the mechanisms of energy homeostasis in cells.
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Acetylation of lysine residues on histone tails reduces histone-DNA affinity, contributing to a more open chromatin configuration that facilitates transcriptional access to rDNA.
“Acetylation of lysine residues on histone tails reduces the affinity between histones and DNA, contributing to a more open chromatin configuration that facilitates transcriptional access to rDNA [178,179].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [179]
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“Acetylation of lysine residues on histone tails reduces the affinity between histones and DNA, contributing to a more open chromatin configuration that facilitates transcriptional access to rDNA [178,179].”
- Authors
- Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Yasuzawa-Tanaka, K., Kuroda, T., Oie, S., Daitoku, H., Okuwaki, M., Nagata, K., Fukamizu, A., Kimura, K., Shimizu, T., & Yanagisawa, J.
- Affiliations
- University of Tsukuba (JP)
- Yokohama City University (JP)
- Corresponding author
- Yanagisawa, Junn
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 133
- Issue
- 4
- Pages
- 627-639
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2134985597
- Cited by
- 394
- References
- 42
- Citations by year
- 2026: 6 · 2025: 14 · 2024: 12 · 2023: 21 · 2022: 20 · 2021: 17 · 2020: 18 · 2019: 22 · 2018: 21 · 2017: 19 · 2016: 27 · 2015: 29 · 2014: 28 · 2013: 35 · 2012: 25
- FWCI
- 10.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- ribosomal DNA, rRNA transcription, ribosome biogenesis, SIRT1, SUV39H1, H3K9me2, histone deacetylation, NAD+/NADH ratio, transcriptional repression, silent chromatin, energy homeostasis, apoptosis
- MeSH terms
- Histone Methyltransferases, Cell Line, Cell Nucleolus, DNA, Ribosomal, Energy Metabolism, Glucose, Histones, Humans, Methyltransferases, Models, Molecular, Molecular Sequence Data, NAD, Nuclear Proteins, Histone-Lysine N-Methyltransferase, Protein Methyltransferases, Repressor Proteins, Transcription, Genetic, RNA-Binding Proteins, Cell Death, Protein Structure, Tertiary, Gene Silencing, Sirtuins, Multiprotein Complexes, Sirtuin 1
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