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Cited by 392Genomics and Chromatin DynamicsChromatin Remodeling and CancerEpigenetics and DNA Methylation

The roles of histone variants in fine-tuning chromatin organization and function

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Martire, Sara, Banaszynski, Laura A.·2020·Nature Reviews Molecular Cell Biology
DOI 10.1038/s41580-020-0262-8PMC PMC8245300
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Abstract

Histones serve to both package and organize DNA within the nucleus. In addition to histone post-translational modification and chromatin remodelling complexes, histone variants contribute to the complexity of epigenetic regulation of the genome. Histone variants are characterized by a distinct protein sequence and a selection of designated chaperone systems and chromatin remodelling complexes that regulate their localization in the genome. In addition, histone variants can be enriched with specific post-translational modifications, which in turn can provide a scaffold for recruitment of variant-specific interacting proteins to chromatin. Thus, through these properties, histone variants have the capacity to endow specific regions of chromatin with unique character and function in a regulated manner. In this Review, we provide an overview of recent advances in our understanding of the contribution of histone variants to chromatin function in mammalian systems. First, we discuss new molecular insights into chaperone-mediated histone variant deposition. Next, we discuss mechanisms by which histone variants influence chromatin properties such as nucleosome stability and the local chromatin environment both through histone variant sequence-specific effects and through their role in recruiting different chromatin-associated complexes. Finally, we focus on histone variant function in the context of both embryonic development and human disease, specifically developmental syndromes and cancer.

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  • H2A.Z destabilizes nucleosomes and is often found at active promoters and enhancers.

    “H2A.Z has been shown to destabilize nucleosomes and is often found at active promoters and enhancers (71), which we observed in our C1 cluster.”

    From SOX9 reprograms endothelial cells by altering the chromatin landscape (2022) · cites this paper as [71]

    The Nucleosome structure and dynamics section (page not provided) says H2A.Z can destabilize nucleosomes and is deposited at enhancers and promoters. It does not specify that those sites are active, and it notes that homotypic H2A.Z nucleosomes are more stable; the destabilization finding applies to particular nucleosome compositions. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

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Authors
Martire, S., & Banaszynski, L. A.
Affiliations
The University of Texas Southwestern Medical Center (US)
Corresponding author
Banaszynski, Laura A.
ORCID
Venue
Nature Reviews Molecular Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2020-07-14
Volume
21
Issue
9
Pages
522-541
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
DOI
10.1038/s41580-020-0262-8
PMC
PMC8245300
OpenAlex
W3042897759
Cited by
392
References
11
Citations by year
2026: 47 · 2025: 54 · 2024: 78 · 2023: 76 · 2022: 66 · 2021: 54 · 2020: 16
FWCI
5.07
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Reviews Molecular Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R35GM124958)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords
histone variants, chromatin organization, histone chaperone, histone variant deposition, chromatin remodeling complexes, histone modifications, nucleosome stability, epigenetic regulation, embryonic development, developmental syndromes, cancer
MeSH terms
Animals, Chromatin, DNA, DNA Repair, Histones, Humans, Nucleosomes, Protein Processing, Post-Translational, Transcription Factors, Transcription, Genetic, Molecular Chaperones, Epigenesis, Genetic

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