ArticleThe Journal of biological chemistry2010
Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
39 citing papers in PubMed, 82 citations in OpenAlex.
- Regulation of central carbon metabolism and storage polymers by PTSApplied and environmental microbiology · 2026Article
- Article
- Ethylene signals through an ethylene receptor to modulate biofilm formation and root colonization in a beneficial plant-associated bacterium.PLoS genetics · 2025Article
- The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria.Frontiers in microbiology · 2024Article
- Enhanced production of polyhydroxyalkanoate with manipulable and reproducible 3-hydroxyvalerate fraction by high alcohol tolerant Cupriavidus malaysiensis USMAA2-4 transformant.Bioprocess and biosystems engineering · 2022Article
- Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021Review
- The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs fromInternational journal of molecular sciences · 2021Article
- Expression of the ace operon in Escherichia coli is triggered in response to growth rate-dependent flux-signal of ATP.FEMS microbiology letters · 2021Article
- Imbalance in Carbon and Nitrogen Metabolism in Comamonas testosteroni R2 Is Caused by Negative Feedback and Rescued by L-arginine.Microbes and environments · 2021Article
- Small but Smart: On the Diverse Role of Small Proteins in the Regulation of Cyanobacterial Metabolism.Life (Basel, Switzerland) · 2020Review
- Complete Genome Sequence of Lactobacillus hilgardii LMG 7934, Carrying the Gene Encoding for the Novel PII-Like Protein PotN.Current microbiology · 2020Article
- Global control of bacterial nitrogen and carbon metabolism by a PTSProceedings of the National Academy of Sciences of the United States of America · 2020Article
- PII Signal Transduction Protein GlnK Alleviates Feedback Inhibition ofApplied and environmental microbiology · 2020Article
- The Human UGT2B7 Nanodisc.Drug metabolism and disposition: the biological fate of chemicals · 2020Article
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Ranking network mechanisms by how they fit diverse experiments and deciding onNPJ systems biology and applications · 2019Article
- Biosensors-Based In Vivo Quantification of 2-Oxoglutarate in Cyanobacteria and Proteobacteria.Life (Basel, Switzerland) · 2018Article
- Fourier Transform-Ion Mobility-Orbitrap Mass Spectrometer: A Next-Generation Instrument for Native Mass Spectrometry.Analytical chemistry · 2018Article
- PProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The PII signaling protein from red algae represents an evolutionary link between cyanobacterial and Chloroplastida PII proteins.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
P(II) proteins are one of the most widespread families of signal transduction proteins in nature, being ubiquitous throughout bacteria, archaea, and plants. They play a major role in coordinating nitrogen metabolism by interacting with, and regulating the activities of, a variety of enzymes, transcription factors, and membrane transport proteins. The regulatory properties of P(II) proteins derive from their ability to bind three effectors: ATP, ADP, and 2-oxoglutarate. However, a clear model to integrate physiological changes with the consequential structural changes that mediate P(II) interaction with a target protein has so far not been developed. In this study, we analyzed the fluctuations in intracellular effector pools in Escherichia coli during association and dissociation of the P(II) protein GlnK with the ammonia channel AmtB. We determined that key features promoting AmtB-GlnK complex formation are the rapid drop in the 2-oxoglutarate pool upon ammonium influx and a simultaneous, but transient, change in the ATP/ADP ratio. We were also able to replicate AmtB-GlnK interactions in vitro using the same effector combinations that we observed in vivo. This comprehensive data set allows us to propose a model that explains the way in which interactions between GlnK and its effectors influence the conformation of GlnK and thereby regulate its interaction with AmtB.
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Registered trials
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.