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TitleStructural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.
Journal, issue, pagesNucleic Acids Res, Vol. 52, Issue 12, Page 7305-7320, Year 2024
Publish dateJul 8, 2024
AuthorsMarkéta Šoltysová / Jana Škerlová / Petr Pachl / Karel Škubník / Milan Fábry / Irena Sieglová / Martina Farolfi / Irina Grishkovskaya / Michal Babiak / Jiří Nováček / Libor Krásný / Pavlína Řezáčová /
PubMed AbstractThe 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 ...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.
External linksNucleic Acids Res / PubMed:38842936 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.7 - 4.4 Å
Structure data

18864

8r3g

EMDB-18864, PDB-8r3g:
Central glycolytic genes regulator (CggR) bound to DNA operator
Method: EM (single particle) / Resolution: 4.4 Å

PDB-8r7y:
Deoxyribonucleoside regulator DeoR in complex with the DNA operator
Method: X-RAY DIFFRACTION / Resolution: 3.7 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bacillus subtilis (bacteria)
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
KeywordsDNA BINDING PROTEIN / Bacillus subtilis / transcription repressor / glucose catabolism / SorC family / transcriptional repressor / protein-DNA complex

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