ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural basis for the allosteric control of the global transcription factor NtcA by the nitrogen starvation signal 2-oxoglutarate.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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60 citing papers in PubMed, 121 citations in OpenAlex.
- Deletion of the gene for a cyanobacterial ribosome-associated protein affects the carbon/nitrogen metabolism.bioRxiv : the preprint server for biology · 2026Article
- A transcriptional biosensor reveals mechanisms of α-ketoglutarate signaling to chromatin.Science (New York, N.Y.) · 2026Article
- Coordination of NProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Structure-Based Analysis of the Evolution of Transcription Factors of the FNR/CRP Family.Biomolecules · 2026Review
- Encapsulins in Terpene Biosynthesis: Enzyme Nanoreactors in Bacterial Secondary Metabolism.Biochemistry · 2026Review
- Carbon metabolism shapes FtsZ levels and cell division in the cyanobacterium Anabaena PCC 7120.Communications biology · 2025Article
- Controlled burn: interconnections between energy-spilling pathways and metabolic signaling in bacteria.Journal of bacteriology · 2025Review
- Structures of the cyanobacterial nitrogen regulators NtcA and PipX complexed to DNA shed light on DNA binding by NtcA and implicate PipX in the recruitment of RNA polymerase.Nucleic acids research · 2025Article
- Temperature changes are signaled in cyanobacteria through the PipX interaction network.Frontiers in microbiology · 2025Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.Nature communications · 2024Article
- Studies on the PII-PipX-NtcA Regulatory Axis of Cyanobacteria Provide Novel Insights into the Advantages and Limitations of Two-Hybrid Systems for Protein Interactions.International journal of molecular sciences · 2024Article
- Analysing the Cyanobacterial PipX Interaction Network Using NanoBiT Complementation inInternational journal of molecular sciences · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.bioRxiv : the preprint server for biology · 2024Article
- Unravelling HetC as a peptidase-based ABC exporter driving functional cell differentiation in the cyanobacteriumMicrobiology spectrum · 2024Article
- Allosteric regulation of nitrate transporter NRT via the signaling protein PII.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- DNA looping mediates cooperative transcription activation.Nature structural & molecular biology · 2024Article
- ppGpp accumulation reduces the expression of the global nitrogen homeostasis-modulating NtcA regulon by affecting 2-oxoglutarate levels.Communications biology · 2023Article
- A mechanistic study of the influence of nitrogen and energy availability on the NH4+ sensitivity of nitrogen assimilation in Synechococcus.Journal of experimental botany · 2022Article
- Nitrogen and phosphorus significantly alter growth, nitrogen fixation, anatoxin-a content, and the transcriptome of the bloom-forming cyanobacterium,Frontiers in microbiology · 2022Article
- Inactivation of Three RG(S/T)GR Pentapeptide-Containing Negative Regulators of HetR Results in Lethal Differentiation ofLife (Basel, Switzerland) · 2020Article
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8 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
2-oxogluatarate (2-OG), a metabolite of the highly conserved Krebs cycle, not only plays a critical role in metabolism, but also constitutes a signaling molecule in a variety of organisms ranging from bacteria to plants and animals. In cyanobacteria, the accumulation of 2-OG constitutes the signal of nitrogen starvation and NtcA, a global transcription factor, has been proposed as a putative receptor for 2-OG. Here we present three crystal structures of NtcA from the cyanobacterium Anabaena: the apoform, and two ligand-bound forms in complex with either 2-OG or its analogue 2,2-difluoropentanedioic acid. All structures assemble as homodimers, with each subunit composed of an N-terminal effector-binding domain and a C-terminal DNA-binding domain connected by a long helix (C-helix). The 2-OG binds to the effector-binding domain at a pocket similar to that used by cAMP in catabolite activator protein, but with a different pattern. Comparative structural analysis reveals a putative signal transmission route upon 2-OG binding. A tighter coiled-coil conformation of the two C-helices induced by 2-OG is crucial to maintain the proper distance between the two F-helices for DNA recognition. Whereas catabolite activator protein adopts a transition from off-to-on state upon cAMP binding, our structural analysis explains well why NtcA can bind to DNA even in its apoform, and how 2-OG just enhances the DNA-binding activity of NtcA. These findings provided the structural insights into the function of a global transcription factor regulated by 2-OG, a metabolite standing at a crossroad between carbon and nitrogen metabolisms.
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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.