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

Autor: Hocher A; Medical Research Council London Institute of Medical Sciences, London, UK. a.hocher@lms.mrc.ac.uk.; Institute of Clinical Sciences, Faculty of Medicine, Imperial College London, London, UK. a.hocher@lms.mrc.ac.uk., Laursen SP; Department of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO, USA., Radford P; School of Life Sciences, Medical School, Queen's Medical Centre, University of Nottingham, Nottingham, UK., Tyson J; School of Life Sciences, Medical School, Queen's Medical Centre, University of Nottingham, Nottingham, UK., Lambert C; School of Life Sciences, Medical School, Queen's Medical Centre, University of Nottingham, Nottingham, UK., Stevens KM; Medical Research Council London Institute of Medical Sciences, London, UK.; Institute of Clinical Sciences, Faculty of Medicine, Imperial College London, London, UK., Montoya A; Medical Research Council London Institute of Medical Sciences, London, UK.; Institute of Clinical Sciences, Faculty of Medicine, Imperial College London, London, UK., Shliaha PV; Medical Research Council London Institute of Medical Sciences, London, UK.; Institute of Clinical Sciences, Faculty of Medicine, Imperial College London, London, UK., Picardeau M; Institut Pasteur, Université Paris Cité, CNRS UMR 6047, Biology of Spirochetes Unit, Paris, France., Sockett RE; School of Life Sciences, Medical School, Queen's Medical Centre, University of Nottingham, Nottingham, UK., Luger K; Department of Biochemistry, University of Colorado Boulder, Boulder, CO, USA. karolin.luger@colorado.edu.; Howard Hughes Medical Institute, Chevy Chase, MD, USA. karolin.luger@colorado.edu., Warnecke T; Medical Research Council London Institute of Medical Sciences, London, UK. tobias.warnecke@lms.mrc.ac.uk.; Institute of Clinical Sciences, Faculty of Medicine, Imperial College London, London, UK. tobias.warnecke@lms.mrc.ac.uk.
Jazyk: angličtina
Zdroj: Nature microbiology [Nat Microbiol] 2023 Nov; Vol. 8 (11), pp. 2006-2019. Date of Electronic Publication: 2023 Oct 09.
DOI: 10.1038/s41564-023-01492-x
Abstrakt: 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.
(© 2023. The Author(s).)
Databáze: MEDLINE
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