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Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.
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- المؤلفون: Šoltysová, Markéta1 (AUTHOR); Škerlová, Jana1 (AUTHOR); Pachl, Petr1 (AUTHOR); Škubník, Karel2 (AUTHOR); Fábry, Milan1 (AUTHOR); Sieglová, Irena1 (AUTHOR); Farolfi, Martina3 (AUTHOR); Grishkovskaya, Irina4 (AUTHOR); Babiak, Michal2 (AUTHOR); Nováček, Jiří2 (AUTHOR); Krásný, Libor3 (AUTHOR); Řezáčová, Pavlína1 (AUTHOR)
- المصدر:
Nucleic Acids Research. 7/8/2024, Vol. 52 Issue 12, p7305-7320. 16p.
- الموضوع:
- معلومة اضافية
- نبذة مختصرة :
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. [ABSTRACT FROM AUTHOR]
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