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Meeting Abstract

Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending

MPS-Authors
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Hu,  Y
Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

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Escudeiro,  P
Protein Bioinformatics Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

/persons/resource/persons271510

Hartmann,  MD       
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

/persons/resource/persons78342

Lupas,  AN       
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

/persons/resource/persons271574

Alva,  V       
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Protein Bioinformatics Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

/persons/resource/persons271242

Hernandez Alvarez,  B       
Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

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https://indico.physik.uni-muenchen.de/event/396/attachments/752/1583/MOM%202024%20Abstract%20Book%20for%20web.pdf
(Abstract)

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Citation

Hu, Y., Schwab, S., Escudeiro, P., van Heesch, T., Vreede, J., Hartmann, M., et al. (2024). Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending. In Molecular Origins of LIFE (pp. 59).


Cite as: https://hdl.handle.net/21.11116/0000-000F-B17F-B
Abstract
Histones are DNA-binding proteins and play a pivotal role in DNA packaging and gene regulation in eukaryotes and archaea. While eukaryotic histones form octamers constituting the nucleosome core, archaeal histones assemble into elongated superhelices upon DNA binding. Recently, histone homologues were discovered in bacteria, prompting our investigations into their structural and functional properties. Here, we present the crystal structure of histone HBb from the predatory bacterium Bdellovibrio bacteriovorus in both apo and DNA-bound forms. Our findings demonstrate that dimeric HBb bends DNA upon binding utilizing interaction interfaces akin to its eukaryotic and archaeal counterparts. Employing a range of biophysical and biochemical methods, we confirm HBb’s sequence-independent DNA binding and compaction by bending. Moreover, we unveil ge- nome-wide binding of HBb across B. bacteriovorus DNA, and show that HBb is essential for bacte- rial survival, suggesting a role in DNA organization and gene regulation. The distinct DNA-binding properties of the bacterial histone HBb, which show similarities yet distinct differences from their archaeal and eukaryotic counterparts, highlight the diverse functions of histones in DNA organiza- tion across all domains of life.