| Autor: |
Jakob, Sara, Steinchen, Wieland, Hanßmann, Juri, Rosum, Julia, Langenfeld, Katja, Osorio-Valeriano, Manuel, Steube, Niklas, Giammarinaro, Pietro I., Hochberg, Georg K. A., Glatter, Timo, Bange, Gert, Diepold, Andreas, Thanbichler, Martin |
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| Zdroj: |
Nature Communications; 1/5/2024, Vol. 15 Issue 1, p1-18, 18p |
| Abstrakt: |
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. Protein VirB regulates the expression of virulence genes in the pathogen Shigella flexneri by binding to DNA sequences far upstream of their promoters. Here, Jakob et al. show that VirB acts as a CTP-dependent molecular switch that uses a loading-and-sliding mechanism to control transcription of its target genes. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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