ArticleProceedings of the National Academy of Sciences of the United States of America2013
P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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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19 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Carbon signaling protein SbtB possesses atypical redox-regulated apyrase activity to facilitate regulation of bicarbonate transporter SbtA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Increasing the Ascomycin Yield by Relieving the Inhibition of Acetyl/Propionyl-CoA Carboxylase by the Signal Transduction Protein GlnB.Frontiers in microbiology · 2021Article
- 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
- PProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The PFrontiers in molecular biosciences · 2018Review
- Evidence for PII with NAGK interaction that regulates Arg synthesis in the microalga Myrmecia incisa in response to nitrogen starvation.Scientific reports · 2017Article
- Ectopic Expression of PII Induces Stomatal Closure inFrontiers in plant science · 2017Article
- The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Microbiology and molecular biology reviews : MMBR · 2015Review
- Glutamine rapidly induces the expression of key transcription factor genes involved in nitrogen and stress responses in rice roots.BMC genomics · 2015Article
- Identification of a Novel Regulatory Mechanism of Nutrient Transport Controlled by TORC1-Npr1-Amu1/Par32.PLoS genetics · 2015Article
- Review
- Article
- Coordination of microbial metabolism.Nature reviews. Microbiology · 2014Review
- Structural basis and target-specific modulation of ADP sensing by the Synechococcus elongatus PII signaling protein.The Journal of biological chemistry · 2014Article
- Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification.Frontiers in microbiology · 2014Article
- Post-translational modification of P II signal transduction proteins.Frontiers in microbiology · 2014Review
- ATPase as a switch in P(II) signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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3 authors at 1 institution in 1 country.
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Abstract
P(II) proteins are one of the most widespread families of signal transduction proteins in nature, being ubiquitous throughout bacteria, archaea, and plants. In all these organisms, P(II) proteins coordinate many facets of nitrogen metabolism by interacting with and regulating the activities of enzymes, transcription factors, and membrane transport proteins. The primary mode of signal perception by P(II) proteins derives from their ability to bind the effector molecules 2-oxoglutarate (2-OG) and ATP or ADP. The role of 2-OG as an indicator of cellular nitrogen status is well understood, but the function of ATP/ADP binding has remained unresolved. We have now shown that the Escherichia coli P(II) protein, GlnK, has an ATPase activity that is inhibited by 2-OG. Hence, when a drop in the cellular 2-OG pool signals nitrogen sufficiency, 2-OG depletion of GlnK causes bound ATP to be hydrolyzed to ADP, leading to a conformational change in the protein. We propose that the role of ATP/ADP binding in E. coli GlnK is to effect a 2-OG-dependent molecular switch that drives a conformational change in the T loops of the P(II) protein. We have further shown that two other P(II) proteins, Azospirillum brasilense GlnZ and Arabidopsis thaliana P(II), have a similar ATPase activity, and we therefore suggest that this switch mechanism is likely to be a general property of most members of the P(II) protein family.
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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.