ArticleBiochemistry2009
Alpha-ketoglutarate controls the ability of the Escherichia coli PII signal transduction protein to regulate the activities of NRII (NrB but does not control the binding of PII to NRII.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Regulating Effect of Exogenous α-Ketoglutarate on Ammonium Assimilation in Poplar.Molecules (Basel, Switzerland) · 2024Article
- Acetylation coordinates the crosstalk between carbon metabolism and ammonium assimilation in Salmonella enterica.The EMBO journal · 2023Article
- Molecular Mechanism and Agricultural Application of the NifA-NifL System for Nitrogen Fixation.International journal of molecular sciences · 2023Review
- A 3' UTR-derived small RNA connecting nitrogen and carbon metabolism in enteric bacteria.Nucleic acids research · 2022Article
- Potential of Phototrophic Purple Nonsulfur Bacteria to Fix Nitrogen in Rice Fields.Microorganisms · 2021Review
- Master regulator NtrC controls the utilization of alternative nitrogen sources in Pseudomonas stutzeri A1501.World journal of microbiology & biotechnology · 2021Article
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- Interaction of the Nitrogen Regulatory Protein GlnB (PFrontiers in microbiology · 2016Article
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- 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
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
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- Adenylylation of mycobacterial Glnk (PII) protein is induced by nitrogen limitation.Tuberculosis (Edinburgh, Scotland) · 2013Article
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- The auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus.Molecular microbiology · 2012Article
- Negative control in two-component signal transduction by transmitter phosphatase activity.Molecular microbiology · 2011Review
- Mechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
PII signal transduction proteins are among the most widely distributed signaling proteins in nature; these proteins are direct sensors of alpha-ketoglutarate and adenylylate energy charge and control receptors that are signal transduction proteins, metabolic enzymes, or permeases involved in nitrogen metabolism. Prior studies showed that alpha-ketoglutarate regulated the ability of PII to control the activities of glutamine synthetase adenylyltransferase (ATase) but did not affect the ability of PII to bind to ATase. Here, we show that a similar pattern of alpha-ketoglutarate regulation was obtained with another PII receptor, the two-component system transmitter protein NRII (NtrB). Although alpha-ketoglutarate was required for the binding of PII to NRII, PII bound to NRII equally well as the concentration of alpha-ketoglutarate was varied through its physiological range. Variation of the concentration of alpha-ketoglutarate through its physiological range provided dramatic regulation of the ability of PII to activate the phosphatase activity of NRII and controlled the ability of PII to inhibit the autophosphorylation of NRII. Thus, PII control of NRII activities could be dissected into distinct binding and regulation steps, and when present in its physiological concentration range, alpha-ketoglutarate apparently played a role in only the latter step.
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