ArticleMolecular microbiology2008
Two variable active site residues modulate response regulator phosphoryl group stability.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- A clarifying perspective on bacterial pseudo-receiver domains.Journal of bacteriology · 2025Review
- PmrA Mutations in Drug-ResistantMicroorganisms · 2025Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
- General strategies for using amino acid sequence data to guide biochemical investigation of protein function.Biochemical Society transactions · 2022Review
- Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems.mSphere · 2021Article
- 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
- Deciphering the Che2 chemosensory pathway and the roles of individual Che2 proteins from Pseudomonas aeruginosa.Molecular microbiology · 2021Article
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- A gated relaxation oscillator mediated by FrzX controls morphogenetic movements in Myxococcus xanthus.Nature microbiology · 2018Article
- Article
- An Adaptive Mutation in Enterococcus faecium LiaR Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes LiaR in an Activated State.Journal of molecular biology · 2016Article
- A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Biochemistry · 2016Article
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
- Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.Journal of bacteriology · 2016Article
- Regulation of Virulence in Staphylococcus aureus: Molecular Mechanisms and Remaining Puzzles.Cell chemical biology · 2016Review
- Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction.Biochemistry · 2015Article
- Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution.Journal of bacteriology · 2015Article
- Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Biochemistry · 2015Article
- Fundamental constraints on the abundances of chemotaxis proteins.Biophysical journal · 2015Article
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Authors and funding
3 authors.
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Abstract
Many signal transduction networks control their output by switching regulatory elements on or off. To synchronize biological response with environmental stimulus, switching kinetics must be faster than changes in input. Two-component regulatory systems (used for signal transduction by bacteria, archaea and eukaryotes) switch via phosphorylation or dephosphorylation of the receiver domain in response regulator proteins. Although receiver domains share conserved active site residues and similar three-dimensional structures, rates of self-catalysed dephosphorylation span a >or= 40,000-fold range in response regulators that control diverse biological processes. For example, autodephosphorylation of the chemotaxis response regulator CheY is 640-fold faster than Spo0F, which controls sporulation. Here we demonstrate that substitutions at two variable active site positions decreased CheY autodephosphorylation up to 40-fold and increased the Spo0F rate up to 110-fold. Particular amino acids had qualitatively similar effects in different response regulators. However, mutant proteins matched to other response regulators at the two key variable positions did not always exhibit similar autodephosphorylation kinetics. Therefore, unknown factors also influence absolute rates. Understanding the effects that particular active site amino acid compositions have on autodephosphorylation rate may allow manipulation of phosphoryl group stability for useful purposes, as well as prediction of signal transduction kinetics from amino acid sequence.
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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.