Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus
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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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Thank you for sharing this interesting study into the molecular basis of histone-DNA interaction in bacteria! It may be possible to further strengthen your conclusions regarding in vitro DNA-histone filament formation using dynamic light scattering. This may also enable you to determine how the length of DNA correlates with histone-DNA fibril formation and stability of these interactions over time. Out of curiosity, have attempted binding assays with a different DNA substrates (especially methylated DNA) to evaluate its effect on fibril formation?
This is an archived comment originally from Januka Athukoralage
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Thank you for sharing this interesting study into the molecular basis of histone-DNA interaction in bacteria! It may be possible to further strengthen your conclusions regarding in vitro DNA-histone filament formation using dynamic light scattering. This may also enable you to determine how the length of DNA correlates with histone-DNA fibril formation and stability of these interactions over time. Out of curiosity, have attempted binding assays with a different DNA substrates (especially methylated DNA) to evaluate its effect on fibril formation?
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