Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus

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...

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Veröffentlicht in:Nature microbiology 2023-11, Vol.8 (11), p.2006-2019
Hauptverfasser: Hocher, Antoine, Laursen, Shawn P., Radford, Paul, Tyson, Jess, Lambert, Carey, Stevens, Kathryn M., Montoya, Alex, Shliaha, Pavel V., Picardeau, Mathieu, Sockett, R. Elizabeth, Luger, Karolin, Warnecke, Tobias
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Sprache:eng
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Zusammenfassung: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 (
ISSN:2058-5276
2058-5276
DOI:10.1038/s41564-023-01492-x