Cited by 236Nuclear Structure and FunctionDNA Repair MechanismsGenomics and Chromatin Dynamics

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Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice

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Krishnan, Vaidehi, Chow, Maggie Zi Ying, Wang, Zimei, Zhang, Le, Liu, Baohua, Liu, Xinguang, Zhou, Zhongjun·2011·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1102789108PMC PMC3145730

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Abstract

Specific point mutations in lamin A gene have been shown to accelerate aging in humans and mice. Particularly, a de novo mutation at G608G position impairs lamin A processing to produce the mutant protein progerin, which causes the Hutchinson Gilford progeria syndrome. The premature aging phenotype of Hutchinson Gilford progeria syndrome is largely recapitulated in mice deficient for the lamin A-processing enzyme, Zmpste24. We have previously reported that Zmpste24 deficiency results in genomic instability and early cellular senescence due to the delayed recruitment of repair proteins to sites of DNA damage. Here, we further investigate the molecular mechanism underlying delayed DNA damage response and identify a histone acetylation defect in Zmpste24 −/− mice. Specifically, histone H4 was hypoacetylated at a lysine 16 residue (H4K16), and this defect was attributed to the reduced association of a histone acetyltransferase, Mof, to the nuclear matrix. Given the reversible nature of epigenetic changes, rescue experiments performed either by Mof overexpression or by histone deacetylase inhibition promoted repair protein recruitment to DNA damage sites and substantially ameliorated aging-associated phenotypes, both in vitro and in vivo. The life span of Zmpste24 −/− mice was also extended with the supplementation of a histone deacetylase inhibitor, sodium butyrate, to drinking water. Consistent with recent data showing age-dependent buildup of unprocessable lamin A in physiological aging, aged wild-type mice also showed hypoacetylation of H4K16. The above results shed light on how chromatin modifications regulate the DNA damage response and suggest that the reversal of epigenetic marks could make an attractive therapeutic target against laminopathy-based progeroid pathologies.

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Authors: Krishnan, V., Chow, M. Z. Y., Wang, Z., Zhang, L., Liu, B., Liu, X., & Zhou, Z.
Affiliations: National University of Singapore (SG)
University of Hong Kong (HK)
Shenzhen University (CN)
Guangdong Medical College (CN)
ORCID: Krishnan, Vaidehi
Wang, Zimei
Zhang, Le
Liu, Baohua
Liu, Xinguang
Zhou, Zhongjun
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2011-07-11
Volume: 108
Issue: 30
Pages: 12325-12330
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1102789108
PMC: PMC3145730
OpenAlex: W2162996266
Cited by: 236
References: 56
Citations by year: 2026: 13 · 2025: 8 · 2024: 12 · 2023: 8 · 2022: 11 · 2021: 15 · 2020: 19 · 2019: 15 · 2018: 21 · 2017: 11 · 2016: 20 · 2015: 21 · 2014: 18 · 2013: 19 · 2012: 22
FWCI: 8.04
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
National University of Singapore (submittedVersion)
The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
Funders: National Natural Science Foundation of China (30871440, 30672205, 9252402301000002)
Natural Science Foundation of Guangdong Province (9252402301000002)
Innovation and Technology Fund
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: ZMPSTE24, Hutchinson-Gilford progeria syndrome, premature senescence, DNA repair, DNA damage response, histone deacetylase inhibition, sodium butyrate, laminopathies, premature aging, chromatin modification, nuclear matrix, genomic instability
MeSH terms: Tumor Suppressor p53-Binding Protein 1, Acetylation, Aging, Animals, Cells, Cultured, Chromosomal Proteins, Non-Histone, Disease Models, Animal, DNA Repair, DNA-Binding Proteins, Histones, Humans, Lysine, Membrane Proteins, Metalloendopeptidases, Nuclear Proteins, Protein Precursors, Nuclear Matrix, Cellular Senescence, Mice, Knockout, Aging, Premature, RNA, Small Interfering, Lamin Type A, Mice, Histone Acetyltransferases, Histone Deacetylase Inhibitors

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Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice

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