ArticleJournal of bacteriology2020
Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.
Article in Journal of bacteriology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- The protein-water H-bond network for bacterial response regulator REC domain activation.Journal of structural biology: X · 2026Article
- A clarifying perspective on bacterial pseudo-receiver domains.Journal of bacteriology · 2025Review
- PmrA Mutations in Drug-ResistantMicroorganisms · 2025Article
- Characterization of two co-regulated response regulators inJournal of bacteriology · 2025Article
- Residue coevolution and mutational landscape for OmpR and NarL response regulator subfamilies.Biophysical journal · 2024Article
- General strategies for using amino acid sequence data to guide biochemical investigation of protein function.Biochemical Society transactions · 2022Review
- Generalizable strategy to analyze domains in the context of parent protein architecture: A CheW case study.Proteins · 2022Article
- Azorhizobium caulinodans Chemotaxis Is Controlled by an Unusual Phosphorelay Network.Journal of bacteriology · 2022Article
- Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems.mSphere · 2021Article
- Reconstitution of an intact clock reveals mechanisms of circadian timekeeping.Science (New York, N.Y.) · 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
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Microorganisms and plants utilize two-component systems to regulate adaptive responses to changing environmental conditions. Sensor kinases detect stimuli and alter their autophosphorylation activity accordingly. Signal propagation occurs via the transfer of phosphoryl groups from upstream kinases to downstream response regulator proteins. Removal of phosphoryl groups from the response regulator typically resets the system. Members of the same protein family may catalyze phosphorylation and dephosphorylation reactions with different efficiencies, exhibiting rate constants spanning many orders of magnitude to accommodate response time scales from milliseconds to days. We previously found that variable positions one or two residues to the C-terminal side of the conserved Asp phosphorylation site (D+2) or Thr/Ser (T+1/T+2) in response regulators alter reaction kinetics by direct interaction with phosphodonor or phosphoacceptor molecules. Here, we explore the kinetic effects of amino acid substitutions at the two positions immediately C-terminal to the conserved Lys (K+1/K+2) in the model
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Registered trials
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.