Histone Variants

A special issue of Epigenomes (ISSN 2075-4655).

Deadline for manuscript submissions: 30 September 2024 | Viewed by 727

Special Issue Editor


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Guest Editor
Division of Environmental Medicine, Department of Medicine, New York University Grossman School of Medicine, New York, NY 10010, USA
Interests: environmental epigenetics; histone variant; chromatin; environmental carcinogenesis; heavy metal; aldehyde

Special Issue Information

Dear Colleagues,

Histone proteins wrap around DNA, forming nucleosomes that serve to package and organize DNA within the nucleus while controlling its accessibility.

In addition to the canonical histones, there are variant histones that possess distinct gene and mRNA structures, as well as unique amino acid sequences compared with their canonical counterparts. Unlike canonical histones, which are primarily expressed during the S phase and deposited onto chromatin through a replication-coupled mechanism, histone variants are expressed throughout the cell cycle and deposited at specific genomic locations via a replication-independent process, facilitated by variant-specific histone chaperones.

Replacing canonical histones with variant histones within a nucleosome imparts unique properties to the nucleosomes, influencing chromatin stability, dynamics, and organization. Histone variants have been shown to play pivotal roles in processes such as transcription, DNA replication and repair, chromosome segregation, and those related to development, aging, and diseases like cancer.

This Special Issue is focused on the latest advances in our understanding of various aspects related to histone variants. We welcome submissions of reviews, research articles, and method manuscripts that offer exceptional insights into the following topics:

  1. Histone variants, their chaperones, and deposition mechanisms.
  2. Post-translational modifications of histone variants.
  3. Histone variants in regulating nucleosome stability, structure, and function.
  4. Histone variants in genome integrity and epigenetic memory.
  5. Alterations in histone variants in response to environmental exposures.
  6. Histone variants in development, aging, and disease.

Dr. Chunyuan Jin
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Epigenomes is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1500 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • histone variant
  • epigenetics
  • chaperone
  • chromatin
  • nucleosome
  • assembly
  • post-translational modification
  • gene expression
  • replication-independent

Published Papers (1 paper)

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Research

13 pages, 3662 KiB  
Article
Structural and Biochemical Characterization of the Nucleosome Containing Variants H3.3 and H2A.Z
by Harry Jung, Vladyslava Sokolova, Gahyun Lee, Victoria Rose Stevens and Dongyan Tan
Epigenomes 2024, 8(2), 21; https://doi.org/10.3390/epigenomes8020021 - 27 May 2024
Viewed by 325
Abstract
Variant H3.3, along with H2A.Z, is notably enriched at promoter regions and is commonly associated with transcriptional activation. However, the specific molecular mechanisms through which H3.3 influences chromatin dynamics at transcription start sites, and its role in gene regulation, remain elusive. Using a [...] Read more.
Variant H3.3, along with H2A.Z, is notably enriched at promoter regions and is commonly associated with transcriptional activation. However, the specific molecular mechanisms through which H3.3 influences chromatin dynamics at transcription start sites, and its role in gene regulation, remain elusive. Using a combination of biochemistry and cryo-electron microscopy (cryo-EM), we show that the inclusion of H3.3 alone does not induce discernible changes in nucleosome DNA dynamics. Conversely, the presence of both H3.3 and H2A.Z enhances DNA’s flexibility similarly to H2A.Z alone. Interestingly, our findings suggest that the presence of H3.3 in the H2A.Z nucleosome provides slightly increased protection to DNA at internal sites within the nucleosome. These results imply that while H2A.Z at active promoters promotes the formation of more accessible nucleosomes with increased DNA accessibility to facilitate transcription, the simultaneous presence of H3.3 offers an additional mechanism to fine-tune nucleosome accessibility and the chromatin environment. Full article
(This article belongs to the Special Issue Histone Variants)
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