Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function
| Autoři | |
|---|---|
| Rok publikování | 2024 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Nucleic acids research |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | https://academic.oup.com/nar/article/52/12/7305/7688987?login=true |
| Doi | http://dx.doi.org/10.1093/nar/gkae434 |
| Klíčová slova | CENTRAL GLYCOLYTIC GENES; EFFECTOR-BINDING DOMAIN; SUBTILIS RNA-POLYMERASE; NUPC-PDP OPERON; BACILLUS-SUBTILIS; TRANSCRIPTIONAL REGULATION; KLEBSIELLA-PNEUMONIAE; CRYSTAL-STRUCTURES; DEOR REPRESSOR; CCP4 SUITE |
| Popis | 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. |
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