Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses.
Shoko SatoMariko DacherHitoshi KurumizakaPublished in: Epigenomes (2022)
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.
Keyphrases
- circulating tumor
- single molecule
- cell free
- dna methylation
- transcription factor
- endothelial cells
- gene expression
- human health
- dna damage
- risk assessment
- nucleic acid
- lymph node
- high resolution
- amino acid
- genetic diversity
- circulating tumor cells
- artificial intelligence
- mass spectrometry
- induced pluripotent stem cells
- big data
- drug induced
- molecular dynamics simulations
- copy number
- multidrug resistant