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Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

期刊

EPIGENOMES
卷 6, 期 3, 页码 -

出版社

MDPI
DOI: 10.3390/epigenomes6030022

关键词

nucleosome; chromatin; parasite; DNA virus

资金

  1. JSPS KAKENHI [JP22K06179, JP20H00449, JP18H05534]
  2. Sumitomo Foundation [21049]
  3. Research Support Project for Life Science and Drug Discovery (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED [JP22ama121009]
  4. JST ERATO [JPMJER1901]

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In this article, the authors review the structures and biophysical properties of nucleosomes containing histones from human parasites and viral histone-like proteins. The data presented confirm the sharing of the overall DNA compaction system among evolutionarily distant species and clarify the deviations from the species-specific nature of the nucleosome.
In eukaryotes, genomic DNA is bound with histone proteins and packaged into chromatin. The nucleosome, a fundamental unit of chromatin, regulates the accessibility of DNA to enzymes involved in gene regulation. During the past few years, structural analyses of chromatin architectures have been limited to evolutionarily related organisms. The amino acid sequences of histone proteins are highly conserved from humans to yeasts, but are divergent in the deeply branching protozoan groups, including human parasites that are directly related to human health. Certain large DNA viruses, as well as archaeal organisms, contain distant homologs of eukaryotic histone proteins. The divergent sequences give rise to unique and distinct nucleosome architectures, although the fundamental principles of histone folding and DNA contact are highly conserved. In this article, we review the structures and biophysical properties of nucleosomes containing histones from the human parasites Giardia lamblia and Leishmania major, and histone-like proteins from the Marseilleviridae amoeba virus family. The presented data confirm the sharing of the overall DNA compaction system among evolutionally distant species and clarify the deviations from the species-specific nature of the nucleosome.

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