Structural basis for cAMP-mediated allosteric control of the catabolite activator protein

Popovych, Nataliya; Tzeng, Shiou‐Ru; Tonelli, Marco; Ebright, Richard H.; Kalodimos, Charalampos G.

doi:10.1073/pnas.0900595106

Cited by 203 publications

(292 citation statements)

References 36 publications

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“…Right, cAMP activation of CRP. The CRP structures are those for E. coli [31,32]. cAMP levels were shown in a cyanobacteria to vary with several external stimuli, including changes from light to darkness [33].…”

Section: Introductionmentioning

confidence: 99%

SPR analysis of promoter binding of Synechocystis PCC6803 transcription factors NtcA and CRP suggests cross‐talk and sheds light on regulation by effector molecules

2014

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Edited by Miguel De la RosaKeywords: Protein-protein interaction PipX protein 2-Oxoglutarate Cyanobacteria Catabolite gene activator protein Nitrogen metabolism a b s t r a c t Surface plasmon resonance monitoring of the binding of transcription factors cAMP receptor protein (CRP) and nitrogen control factor of cyanobacteria (NtcA) from Synechocystis sp. PCC6803 to promoter fragments of glnA, glnN (NtcA regulon) and cccS (CRP regulon), revealed exclusive CRP binding to cccS, whereas NtcA was bound to all three promoters with different affinities, which were strongly increased by the NtcA activator 2-oxoglutarate. Effective NtcA affinity for 2-oxoglutarate varied with the promoter. High-affinity promoters and the NtcA-coactivating protein PII-interacting protein X (PipX) increased NtcA affinity towards 2-oxoglutarate, suggesting PipX-stabilization of the 2-oxoglutarate-bound NtcA conformation. PipX binding to NtcA required 2-oxoglutarate and was much tighter (K d % 85 nM) than to the PipX-sequestering PII protein. NtcA appears to require more strongly PipX and 2-oxoglutarate (2OG) for estimulating gene expression at promoters having ''imperfect'' NtcA binding sites.

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Section: Introductionmentioning

confidence: 99%

SPR analysis of promoter binding of Synechocystis PCC6803 transcription factors NtcA and CRP suggests cross‐talk and sheds light on regulation by effector molecules

2014

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“…Each subunit contains a cAMP-binding domain (CBD) mediating dimerization and a DNA-binding domain (DBD). cAMP elicits a coil-to-helix transition in CAP positioning the recognition helices in the DBDs in the appropriate orientation interacting with the successive major groves of DNA (Popovych et al, 2009). The symmetric CAP dimer binds two molecules of cAMP with strong negative cooperativity.…”

Section: Structural Symmetry and Transient Asymmetry Of Signalling Prmentioning

confidence: 99%

Asymmetric perturbations of signalling oligomers

Maksay

Tőke

2014

Progress in Biophysics and Molecular Biology

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This review focuses on rapid and reversible noncovalent interactions for symmetric oligomers of tetramers (voltage-gated cation channels, ionotropic glutamate receptor, CNG and CHN channels); pentameric ligand-gated and mechanosensitive channels; higher order oligomers (gap junction channel, chaperonins, proteasome, virus capsid); as well as primary and secondary transporters. In conclusion, asymmetric perturbations seem to play important functional roles in a broad range of communicating networks.

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“…The cAMP-mediated allosteric transition in CAP that activates the protein for DNA binding 53 is a characteristic example of the widely held view that allosteric regulation is predominantly structural in origin. The DBD in cAMP-free CAP (apo-CAP) adopts an orientation that is incompatible with DNA binding [ Fig.…”

Section: Dynamic Activation Of Protein Functionmentioning

confidence: 99%

“…55 Determining the chemical shifts of the excited state using relaxation dispersion have in several cases provided information that those states structurally resemble related functional states. 40,53,82,83,87 Incorporation of chemical shifts in NMR structure refinement and the development of new NMR experiments that can report on internuclear vector orientations in excited conformational states provide valuable structural constraints that may enable direct structural characterization of higher energy protein conformations. [88][89][90] Kay and coworkers recently reported the structure of an ''invisible'' protein folding intermediate, a remarkable achievement convincingly showing that structure determination of weakly populated conformational states are within reach.…”

Section: Protein Activation Via Energetically Excited Statesmentioning

confidence: 99%

NMR reveals novel mechanisms of protein activity regulation

Kalodimos

2011

Protein Science

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NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide siteresolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.

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Structural basis for cAMP-mediated allosteric control of the catabolite activator protein

Cited by 203 publications

References 36 publications

SPR analysis of promoter binding of Synechocystis PCC6803 transcription factors NtcA and CRP suggests cross‐talk and sheds light on regulation by effector molecules

SPR analysis of promoter binding of Synechocystis PCC6803 transcription factors NtcA and CRP suggests cross‐talk and sheds light on regulation by effector molecules

Asymmetric perturbations of signalling oligomers

NMR reveals novel mechanisms of protein activity regulation

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