0586786 - ÚOCHB 2025 RIV US eng J - Journal Article
Šoltysová, Markéta - Škerlová, Jana - Pachl, Petr - Škubník, K. - Fábry, Milan - Sieglová, Irena - Farolfi, Martina - Grishkovskaya, I. - Babiak, M. - Nováček, J. - Krásný, Libor - Řezáčová, Pavlína
Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.
Nucleic Acids Research. Roč. 52, č. 12 (2024), s. 7305-7320, č. článku gkae434. ISSN 0305-1048. E-ISSN 1362-4962
R&D Projects: GA MŠMT(CZ) LX22NPO5103; GA MŠMT(CZ) EH22_008/0004575
Institutional support: RVO:61388963 ; RVO:61388971
Impact factor: 14.9, year: 2022
Method of publishing: Open access
https://doi.org/10.1093/nar/gkae434

The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics.
Permanent Link: https://hdl.handle.net/11104/0354179