ArticleNature microbiology2023
Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus.
Article in Nature microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Structure of NO16, a marine non-tailed vibriophage with an unusual symmetry-mismatched vertex arrangement.PLoS pathogens · 2026Article
- Von Willebrand factor A2 domain inhibits A1-DNA binding while preserving A1-platelet interaction under flow: evidence from recombinant domain constructs.Research and practice in thrombosis and haemostasis · 2026Article
- Bdellovibrio and Like Organisms (BALOs): Biology, Predatory Mechanisms, and Bioindustrial Potential.World journal of microbiology & biotechnology · 2026Review
- Histone diversity in the archaeal domain of life.Nature communications · 2026Article
- Insights into FACT in Cancers with Targeted Therapeutic Implications.Molecular and cellular biology · 2026Review
- DNA Wrapping by a tetrameric bacterial histone.Nature communications · 2025Article
- Isolation and partial characterization of antimicrobial peptide-enriched fractions from Parabacteroides distasonis.Scientific reports · 2025Article
- Article
- Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures.Nature communications · 2025Article
- Linking genomic evolutionary transitions to ecological phenotypic adaptations inbioRxiv : the preprint server for biology · 2025Article
- A dynamic histone-based chromatin regulatory toolkit underpins genome and developmental evolution in an invertebrate clade.Genome biology · 2025Article
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- The chromatin landscape of the histone-possessingGenome research · 2025Article
- Using AlphaFold-Multimer to study novel protein-protein interactions of predation essential hypothetical proteins inFrontiers in bioinformatics · 2025Article
- Binding of zebrafish lipovitellin and L1‑ORF2 increases the accessibility of L1‑ORF2 via interference with histone wrapping.International journal of molecular medicine · 2025Article
- Review
- Fantastic proteins and where to find them - histones, in the nucleus and beyond.Journal of cell science · 2024Review
- Characterization of Medusavirus encoded histones reveals nucleosome-like structures and a unique linker histone.Nature communications · 2024Article
- Histones and histone variant families in prokaryotes.Nature communications · 2024Article
- Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending.Nucleic acids research · 2024Article
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
Abstract
Histone proteins bind DNA and organize the genomes of eukaryotes and most archaea, whereas bacteria rely on different nucleoid-associated proteins. Homology searches have detected putative histone-fold domains in a few bacteria, but whether these function like archaeal/eukaryotic histones is unknown. Here we report that histones are major chromatin components in the bacteria Bdellovibrio bacteriovorus and Leptospira interrogans. Patterns of sequence evolution suggest important roles for histones in additional bacterial clades. Crystal structures (<2.0 Å) of the B. bacteriovorus histone (Bd0055) dimer and the histone-DNA complex confirm conserved histone-fold topology but indicate a distinct DNA-binding mode. Unlike known histones in eukaryotes, archaea and viruses, Bd0055 binds DNA end-on, forming a sheath of dimers encasing straight DNA rather than wrapping DNA around their outer surface. Our results demonstrate that histones are present across the tree of life and highlight potential evolutionary innovation in how they associate with DNA.
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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 OpenQuestion graph.