The SorC family is a large group of bacterial transcription regulators involved in controlling carbohydrate catabolism and quorum sensing. SorC proteins consist of a conserved C-terminal effector-binding domain and an N-terminal DNA-binding domain, whose type divides the family into two subfamilies: SorC/DeoR and SorC/CggR. Proteins of the SorC/CggR subfamily are known to regulate the key node of glycolysis-triose phosphate interconversion. On the other hand, SorC/DeoR proteins are involved in a variety of peripheral carbohydrate catabolic pathways and quorum sensing functions, including virulence. Despite the abundance and importance of this family, SorC proteins seem to be on the periphery of scientific interest, which might be caused by the fragmentary information about its representatives. This review aims to compile the existing knowledge and provide material to inspire future questions about the SorC protein family.

• Klíčová slova
• SorC family, bacterial transcription regulation, carbohydrate metabolism, quorum sensing,
• MeSH
• Bacteria * metabolismus   genetika   MeSH
• bakteriální proteiny * metabolismus   chemie   genetika   MeSH
• quorum sensing MeSH
• regulace genové exprese u bakterií MeSH
• transkripční faktory * metabolismus   chemie   genetika   MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• bakteriální proteiny * MeSH
• transkripční faktory * MeSH

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.

• MeSH
• Bacillus subtilis * genetika   metabolismus   MeSH
• bakteriální proteiny * chemie   metabolismus   genetika   MeSH
• DNA bakterií metabolismus   chemie   genetika   MeSH
• DNA vazebné proteiny chemie   metabolismus   genetika   MeSH
• DNA chemie   metabolismus   MeSH
• elektronová kryomikroskopie * MeSH
• fruktosadifosfáty MeSH
• krystalografie rentgenová MeSH
• molekulární modely * MeSH
• multimerizace proteinu MeSH
• operon genetika   MeSH
• regulace genové exprese u bakterií MeSH
• represorové proteiny * chemie   metabolismus   genetika   MeSH
• vazba proteinů MeSH
• vazebná místa MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• bakteriální proteiny * MeSH
• DNA bakterií MeSH
• DNA vazebné proteiny MeSH
• DNA MeSH
• fructose-1,6-diphosphate MeSH Prohlížeč
• fruktosadifosfáty MeSH
• represorové proteiny * MeSH