ArticleJournal of bacteriology2004
Mutations altering the N-terminal receiver domain of NRI (NtrC) That prevent dephosphorylation by the NRII-PII complex in Escherichia coli.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Review
- Suppressor mutations reveal an NtrC-like response regulator, NmpR, for modulation of Type-IV Pili-dependent motility in Myxococcus xanthus.PLoS genetics · 2018Article
- Evolutionary implications of Liebig's law of the minimum: Selection under low concentrations of two nonsubstitutable nutrients.Ecology and evolution · 2017Article
- The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates.Scientific reports · 2017Article
- A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Biochemistry · 2016Article
- Article
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
- Missense substitutions reflecting regulatory control of transmitter phosphatase activity in two-component signalling.Molecular microbiology · 2013Article
- Polymyxin resistance of Pseudomonas aeruginosa phoQ mutants is dependent on additional two-component regulatory systems.Antimicrobial agents and chemotherapy · 2013Article
- Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Negative control in two-component signal transduction by transmitter phosphatase activity.Molecular microbiology · 2011Review
- Multi-scale genetic dynamic modelling II: application to synthetic biology: an algorithmic Markov chain based approach.Theory in biosciences = Theorie in den Biowissenschaften · 2011Article
- Receiver domain structure and function in response regulator proteins.Current opinion in microbiology · 2010Review
- Two variable active site residues modulate response regulator phosphoryl group stability.Molecular microbiology · 2008Article
- Dual involvement of CbrAB and NtrBC in the regulation of histidine utilization in Pseudomonas fluorescens SBW25.Genetics · 2008Article
- Genetic dissection of the divergent activities of the multifunctional membrane sensor BglF.Journal of bacteriology · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The phosphorylated form of NRI is the transcriptional activator of nitrogen-regulated genes in Escherichia coli. NRI approximately P displays a slow autophosphatase activity and is rapidly dephosphorylated by the complex of the NRII and PII signal transduction proteins. Here we describe the isolation of two mutations, causing the alterations DeltaD10 and K104Q in the receiver domain of NRI, that were selected as conferring resistance to dephosphorylation by the NRII-PII complex. The mutations, which alter highly conserved residues near the D54 site of phosphorylation in the NRI receiver domain, resulted in elevated expression of nitrogen-regulated genes under nitrogen-rich conditions. The altered NRI receiver domains were phosphorylated by NRII in vitro but were defective in dephosphorylation. The DeltaD10 receiver domain retained normal autophosphatase activity but was resistant to dephosphorylation by the NRII-PII complex. The K104Q receiver domain lacked both the autophosphatase activity and the ability to be dephosphorylated by the NRII-PII complex. The properties of these altered proteins are consistent with the hypothesis that the NRII-PII complex is not a true phosphatase but rather collaborates with NRI approximately P to bring about its dephosphorylation.
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