ArticleBiophysical journal2007
Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.Nucleic acids research · 2024Article
- Studying Macromolecular Interactions of Cellular Machines by the Combined Use of Analytical Ultracentrifugation, Light Scattering, and Fluorescence Spectroscopy Methods.Advances in experimental medicine and biology · 2024Article
- Measuring glycolytic flux in single yeast cells with an orthogonal synthetic biosensor.Molecular systems biology · 2019Article
- Transcriptional regulation is insufficient to explain substrate-induced flux changes in Bacillus subtilis.Molecular systems biology · 2013Article
- 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
- Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO.Biophysical reviews · 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
- Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Comparison of the regulation, metabolic functions, and roles in virulence of the glyceraldehyde-3-phosphate dehydrogenase homologues gapA and gapB in Staphylococcus aureus.Infection and immunity · 2010Article
- Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex.Nucleic acids research · 2010Article
- Characterization of the control catabolite protein of gluconeogenic genes repressor by fluorescence cross-correlation spectroscopy and other biophysical approaches.Biophysical journal · 2008Article
- 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.Molecular microbiology · 2008Article
- Transcriptomic and phenotypic analyses suggest a network between the transcriptional regulators HrcA and sigmaB in Listeria monocytogenes.Applied and environmental microbiology · 2007Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The central glycolytic genes repressor (CggR) controls the transcription of the gapA operon encoding five key glycolytic enzymes in Bacillus subtilis. CggR recognizes a unique DNA target sequence comprising two direct repeats and fructose-1,6-bisphosphate (FBP) is the inducer that negatively controls this interaction. We present here analytical ultracentrifugation and fluorescence anisotropy experiments that demonstrate that CggR binds as a tetramer to the full-length operator DNA in a highly cooperative manner. We also show that CggR binds as a dimer to each direct repeat, the affinity being approximately 100-fold higher for the 3' repeat. In addition, our studies reveal a bimodal effect of FBP on the repressor/operator interaction. At micromolar concentrations, FBP leads to a change in the conformational dynamics of the complex. In the millimolar range, without altering the stoichiometry, FBP leads to a drastic reduction in the affinity and cooperativity of the complex. This bimodal response suggests the existence of two sugar-binding sites in the repressor, a high affinity site at which FBP acts as a structural co-factor and a low affinity site underlying the molecular mechanism of gapA induction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.