ArticleNature communications2025
DNA Wrapping by a tetrameric bacterial histone.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Article
- 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
- The Expanding Histone Universe: Histone-Based DNA Organization in Noneukaryotic Organisms.Annual review of biophysics · 2026Review
- Histone diversity in the archaeal domain of life.Nature communications · 2026Article
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Authors and funding
12 authors.
Funding
Abstract
Histones are conserved DNA-packaging proteins found across all domains of life. In eukaryotes, canonical histones form octamers that wrap ~147 base pairs (bp) of DNA into nucleosomes, while in archaea they form dimers that polymerize into extended hypernucleosomes. Although bacteria were long thought to lack histones, homologs have now been identified in diverse lineages. We previously characterized the histone HBb from Bdellovibrio bacteriovorus, which binds and bends DNA as a dimer. Here, we describe HLp from Leptospira perolatii and show by crystallographic and biophysical analyses that, unlike HBb, it forms stable tetramers and binds DNA nonspecifically, wrapping ~60 bp of DNA around its core. Molecular dynamics simulations, DNA-binding assays, and heterologous expression in Escherichia coli, where HLp reorganizes the nucleoid, support a role in bacterial chromatin organization. These findings expand the repertoire of bacterial histone-DNA interactions and highlight the diversity of histone-based genome organization across the tree of life.
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Registered trials
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