ArticleJournal of bacteriology2003
Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein.
Article in Journal of bacteriology, 2003. 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, 39 citations in OpenAlex.
- Constitutive activation of two-component systems reveals regulatory network interactions in Streptococcus agalactiae.Nature communications · 2024Article
- Bacterial Histidine Kinase and the Development of Its Inhibitors in the 21st Century.Antibiotics (Basel, Switzerland) · 2024Review
- EnvZ/OmpR Two-Component Signaling: An Archetype System That Can Function Noncanonically.EcoSal Plus · 2020Review
- The flagellar set Fla2 in Rhodobacter sphaeroides is controlled by the CckA pathway and is repressed by organic acids and the expression of Fla1.Journal of bacteriology · 2015Article
- Genetic analysis of signal integration by the Sinorhizobium meliloti sensor kinase FeuQ.Microbiology (Reading, England) · 2015Article
- Specificity residues determine binding affinity for two-component signal transduction systems.mBio · 2013Article
- Missense substitutions reflecting regulatory control of transmitter phosphatase activity in two-component signalling.Molecular microbiology · 2013Article
- Genetic and biochemical dissection of a HisKA domain identifies residues required exclusively for kinase and phosphatase activities.PLoS genetics · 2012Article
- Negative control in two-component signal transduction by transmitter phosphatase activity.Molecular microbiology · 2011Review
- Changes of curdlan biosynthesis and nitrogenous compounds utilization characterized in ntrC mutant of Agrobacterium sp. ATCC 31749.Current microbiology · 2011Article
- Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain.Journal of bacteriology · 2010Article
- How important is the phosphatase activity of sensor kinases?Current opinion in microbiology · 2010Review
- Global regulation of gene expression and cell differentiation in Caulobacter crescentus in response to nutrient availability.Journal of bacteriology · 2010Article
- Asymmetric cross-regulation between the nitrate-responsive NarX-NarL and NarQ-NarP two-component regulatory systems from Escherichia coli K-12.Molecular microbiology · 2010Article
- Article
- In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine.Journal of bacteriology · 2007Article
- Using two-component systems and other bacterial regulatory factors for the fabrication of synthetic genetic devices.Methods in enzymology · 2007Article
- Mutations altering the N-terminal receiver domain of NRI (NtrC) That prevent dephosphorylation by the NRII-PII complex in Escherichia coli.Journal of bacteriology · 2004Article
- Yeast two-hybrid studies on interaction of proteins involved in regulation of nitrogen fixation in the phototrophic bacterium Rhodobacter capsulatus.Journal of bacteriology · 2003Article
- Identification and analysis of Escherichia coli proteins that interact with the histidine kinase NtrB in a yeast two-hybrid system.Molecular genetics and genomics : MGG · 2003Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutant forms of Escherichia coli NRII (NtrB) were isolated that retained wild-type NRII kinase activity but were defective in the PII-activated phosphatase activity of NRII. Mutant strains were selected as mimicking the phenotype of a strain (strain BK) that lacks both of the related PII and GlnK signal transduction proteins and thus has no mechanism for activation of the NRII phosphatase activity. The selection and screening procedure resulted in the isolation of numerous mutants that phenotypically resembled strain BK to various extents. Mutations mapped to the glnL (ntrB) gene encoding NRII and were obtained in all three domains of NRII. Two distinct regions of the C-terminal, ATP-binding domain were identified by clusters of mutations. One cluster, including the Y302N mutation, altered a lid that sits over the ATP-binding site of NRII. The other cluster, including the S227R mutation, defined a small surface on the "back" or opposite side of this domain. The S227R and Y302N proteins were purified, along with the A129T (NRII2302) protein, which has reduced phosphatase activity due to a mutation in the central domain of NRII, and the L16R protein, which has a mutation in the N-terminal domain of NRII. The S227R, Y302N, and L16R proteins were specifically defective in the PII-activated phosphatase activity of NRII. Wild-type NRII, Y302N, A129T, and L16R proteins bound to PII, while the S227R protein was defective in binding PII. This suggests that the PII-binding site maps to the "back" of the C-terminal domain and that mutation of the ATP-lid, central domain, and N-terminal domain altered functions necessary for the phosphatase activity after PII binding.
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