ArticleJournal of molecular biology2014
Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.
Article in Journal of molecular biology, 2014. 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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Who cites it
19 citing papers in PubMed.
- Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.Nature communications · 2023Article
- Allostery and protein plasticity: the keystones for bacterial signaling and regulation.Biophysical reviews · 2021Review
- Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Biochemistry · 2021Article
- Phospho-dependent signaling during the general stress response by the atypical response regulator and ClpXP adaptor RssB.Protein science : a publication of the Protein Society · 2021Article
- Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator.Nucleic acids research · 2018Article
- TheMicrobiology (Reading, England) · 2017Article
- Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromThe Journal of biological chemistry · 2017Article
- The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates.Scientific reports · 2017Article
- To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Molecular microbiology · 2017Review
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
- Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.Nucleic acids research · 2016Article
- NMR Methods to Study Dynamic Allostery.PLoS computational biology · 2016Review
- Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution.Journal of bacteriology · 2015Article
- A network of molecular switches controls the activation of the two-component response regulator NtrC.Nature communications · 2015Article
- Free energy landscape of activation in a signalling protein at atomic resolution.Nature communications · 2015Article
- The role of protein dynamics in allosteric effects-introduction.Biophysical reviews · 2015Article
- The aspartate-less receiver (ALR) domains: distribution, structure and function.PLoS pathogens · 2015Article
- Ligand-induced folding of a two-component signaling receiver domain.Biochemistry · 2015Article
- Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Frontiers in plant science · 2015Review
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5 authors.
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Abstract
The dominant theory on the mechanism of response regulators activation in two-component bacterial signaling systems is the "Y-T coupling" mechanism, wherein the χ1 rotameric state of a highly conserved aromatic residue correlates with the activation of the protein via structural rearrangements coupled to a conserved tyrosine. In this paper, we present evidence that, in the receiver domain of the response regulator nitrogen regulatory protein C (NtrC(R)), the interconversion of this tyrosine (Y101) between its rotameric states is actually faster than the rate of inactive/active conversion and is not correlated to the activation process. Data gathered from NMR relaxation dispersion experiments show that a subset of residues surrounding the conserved tyrosine sense a process that is occurring at a faster rate than the inactive/active conformational transition. We show that this process is related to χ1 rotamer exchange of Y101 and that mutation of this aromatic residue to a leucine eliminated this second faster process without affecting activation. Computational simulations of NtrC(R) in its active conformation further demonstrate that the rotameric state of Y101 is uncorrelated with the global conformational transition during activation. Moreover, the tyrosine does not appear to be involved in the stabilization of the active form upon phosphorylation and is not essential in propagating the signal downstream for ATPase activity of the central domain. Our data provide experimental evidence against the generally accepted "Y-T coupling" mechanism of activation in NtrC(R).
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