ArticleCommunications biology2023
DNA-bridging by an archaeal histone variant via a unique tetramerisation interface.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- DNA Wrapping by a tetrameric bacterial histone.Nature communications · 2025Article
- Chromatin and gene regulation in archaea.Molecular microbiology · 2025Review
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- The chromatin landscape of the histone-possessingGenome research · 2025Article
- Histones and histone variant families in prokaryotes.Nature communications · 2024Article
- Dual dimeric interactions in the nucleic acid-binding protein Sac10b lead to multiple bridging of double-stranded DNA.Heliyon · 2024Article
- Archaeal histone-based chromatin structures regulate transcription elongation rates.Communications biology · 2024Article
- Cbp1 and Cren7 form chromatin-like structures that ensure efficient transcription of long CRISPR arrays.Nature communications · 2024Article
- Quantitation of DNA Binding Affinity Using Tethered Particle Motion.Methods in molecular biology (Clifton, N.J.) · 2024Article
- How Do Thermophiles Organize Their Genomes?Microbes and environments · 2024Review
- The chromatin landscape of the euryarchaeon Haloferax volcanii.Genome biology · 2023Article
- The landscape of the histone-organized chromatin of Bdellovibrionota bacteria.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, histone paralogues form obligate heterodimers such as H3/H4 and H2A/H2B that assemble into octameric nucleosome particles. Archaeal histones are dimeric and assemble on DNA into 'hypernucleosome' particles of varying sizes with each dimer wrapping 30 bp of DNA. These are composed of canonical and variant histone paralogues, but the function of these variants is poorly understood. Here, we characterise the structure and function of the histone paralogue MJ1647 from Methanocaldococcus jannaschii that has a unique C-terminal extension enabling homotetramerisation. The 1.9 Å X-ray structure of a dimeric MJ1647 species, structural modelling of the tetramer, and site-directed mutagenesis reveal that the C-terminal tetramerization module consists of two alpha helices in a handshake arrangement. Unlike canonical histones, MJ1647 tetramers can bridge two DNA molecules in vitro. Using single-molecule tethered particle motion and DNA binding assays, we show that MJ1647 tetramers bind ~60 bp DNA and compact DNA in a highly cooperative manner. We furthermore show that MJ1647 effectively competes with the transcription machinery to block access to the promoter in vitro. To the best of our knowledge, MJ1647 is the first histone shown to have DNA bridging properties, which has important implications for genome structure and gene expression in archaea.
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