ArticleNature communications2024
Histones and histone variant families in prokaryotes.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed.
- The double histone fold: Structure, functional implications across the tree of life and relevance to protein design.Protein science : a publication of the Protein Society · 2026Review
- Histone diversity in the archaeal domain of life.Nature communications · 2026Article
- Tn-seq of Thermus thermophilus Genome Reveals Unexpected Tolerance to Insertions in Bacterial Common Essential Genes.MicrobiologyOpen · 2026Article
- DNA Wrapping by a tetrameric bacterial histone.Nature communications · 2025Article
- Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures.Nature communications · 2025Article
- Chromatin and gene regulation in archaea.Molecular microbiology · 2025Review
- The chromatin landscape of the histone-possessingGenome research · 2025Article
- Review
- Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending.Nucleic acids research · 2024Article
- Nucleosomes at the Dawn of Eukaryotes.Genome biology and evolution · 2024Review
- The landscape of the histone-organized chromatin of Bdellovibrionota bacteria.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Histones are important chromatin-organizing proteins in eukaryotes and archaea. They form superhelical structures around which DNA is wrapped. Recent studies have shown that some archaea and bacteria contain alternative histones that exhibit different DNA binding properties, in addition to highly divergent sequences. However, the vast majority of these histones are identified in metagenomes and thus are difficult to study in vivo. The recent revolutionary breakthroughs in computational protein structure prediction by AlphaFold2 and RoseTTAfold allow for unprecedented insights into the potential function and structure of previously uncharacterized proteins. Here, we categorize the prokaryotic histone space into 17 distinct groups based on AlphaFold2 predictions. We identify a superfamily of histones, termed α3 histones, which are common in archaea and present in several bacteria. Importantly, we establish the existence of a large family of histones throughout archaea and in some bacteriophages that, instead of wrapping DNA, bridge DNA, thereby diverging from conventional nucleosomal histones.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.