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The virulence regulator VirB from Shigella flexneri uses a CTP-dependent switch mechanism to activate gene expression

MPG-Autoren
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Hanßmann,  Juri
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
external;

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Langenfeld,  Katja
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Steube,  Niklas
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Hochberg,  Georg K. A.       
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Glatter,  Timo       
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Bange,  Gert       
Max Planck Fellow Molecular Physiology of Microbes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
external;

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Diepold,  Andreas       
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thanbichler,  Martin       
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
external;

Externe Ressourcen

https://doi.org/10.1038/s41467-023-44509-z
(Verlagsversion)

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Zitation

Jakob, S., Steinchen, W., Hanßmann, J., Rosum, J., Langenfeld, K., Osorio-Valeriano, M., et al. (2024). The virulence regulator VirB from Shigella flexneri uses a CTP-dependent switch mechanism to activate gene expression. Nature Communications, 15(1): 318. doi:10.1038/s41467-023-44509-z.


Zitierlink: https://hdl.handle.net/21.11116/0000-000E-2030-7
Zusammenfassung
The transcriptional antisilencer VirB acts as a master regulator of virulence gene expression in the human pathogen Shigella flexneri. It binds DNA sequences (virS) upstream of VirB-dependent promoters and counteracts their silencing by the nucleoid-organizing protein H-NS. However, its precise mode of action remains unclear. Notably, VirB is not a classical transcription factor but related to ParB-type DNA-partitioning proteins, which have recently been recognized as DNA-sliding clamps using CTP binding and hydrolysis to control their DNA entry gate. Here, we show that VirB binds CTP, embraces DNA in a clamp-like fashion upon its CTP-dependent loading at virS sites and slides laterally on DNA after clamp closure. Mutations that prevent CTP-binding block VirB loading in vitro and abolish the formation of VirB nucleoprotein complexes as well as virulence gene expression in vivo. Thus, VirB represents a CTP-dependent molecular switch that uses a loading-and-sliding mechanism to control transcription during bacterial pathogenesis.