ArticleMolecular microbiology2008
Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Sugar-sensing swodkoreceptors and swodkocrine signaling.Animal models and experimental medicine · 2025Article
- Tracking fructose 1,6-bisphosphate dynamics in liver cancer cells using a fluorescent biosensor.iScience · 2024Article
- Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.Nucleic acids research · 2024Article
- Phylogeny and structural modeling of the transcription factor CsqR (YihW) from Escherichia coli.Scientific reports · 2024Article
- DeoR regulates lincomycin production in Streptomyces lincolnensis.World journal of microbiology & biotechnology · 2023Article
- The Salmonella T3SS1 effector IpaJ is regulated by ItrA and inhibits the MAPK signaling pathway.PLoS pathogens · 2022Article
- Monitoring glycolytic dynamics in single cells using a fluorescent biosensor for fructose 1,6-bisphosphate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Measuring glycolytic flux in single yeast cells with an orthogonal synthetic biosensor.Molecular systems biology · 2019Article
- Transcriptional control of central carbon metabolic flux in Bifidobacteria by two functionally similar, yet distinct LacI-type regulators.Scientific reports · 2019Article
- Assessing the similarity of ligand binding conformations with the Contact Mode Score.Computational biology and chemistry · 2016Article
- The SARP Family Regulator Txn9 and Two-Component Response Regulator Txn11 are Key Activators for Trioxacarcin Biosynthesis in Streptomyces bottropensis.Current microbiology · 2015Article
- The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Protein science : a publication of the Protein Society · 2015Review
- Crystal structures of the LsrR proteins complexed with phospho-AI-2 and two signal-interrupting analogues reveal distinct mechanisms for ligand recognition.Journal of the American Chemical Society · 2013Article
- Structural basis for phosphorylated autoinducer-2 modulation of the oligomerization state of the global transcription regulator LsrR from Escherichia coli.The Journal of biological chemistry · 2013Article
- Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Article
- Changes in the Staphylococcus aureus transcriptome during early adaptation to the lung.PloS one · 2012Article
- Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex.Nucleic acids research · 2010Article
- Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Expression of genes in the gapA operon encoding five enzymes for triose phosphate interconversion in Bacillus subtilis is negatively regulated by the Central glycolytic genes Regulator (CggR). CggR belongs to the large SorC/DeoR family of prokaryotic transcriptional regulators, characterized by an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. When no glucose is present in growth media, CggR binds to its target DNA sequence and blocks the transcription of genes in the gapA operon. In the presence of glucose, binding of the known effector molecule fructose-1,6-bisphosphate abolishes this interaction. We have identified dihydroxyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate as additional CggR ligands that can bind to the effector-binding site. Crystal structures of C-CggR, the C-terminal effector-binding domain of CggR, both unliganded as well as in complex with the four ligands at resolutions between 1.65 and 1.80 A reveal unique ligand-specific structural changes in the binding site that affect the dimer interface. Binding affinities of these ligands were determined by isothermal titration calorimetry. Chemical cross-linking shows that CggR oligomerization is mediated through its effector-binding domain, and that binding of the different ligands differentially affects the distribution of oligomers. Electrophoretic mobility shift assays (EMSAs) confirmed a destabilizing effect of fructose-1,6-bisphosphate on the CggR/DNA complex, and also showed similar effects for dihydroxyacetone phosphate. Our results suggest that CggR stability and function may be modulated by various effectors in a complex fashion.
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