ArticleBiochemistry2014
The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Genome analysis of a halophilicFrontiers in microbiology · 2023Article
- Interdomain Linkers Regulate Histidine Kinase Activity by Controlling Subunit Interactions.Biochemistry · 2022Article
- Engineered chemotaxis core signaling units indicate a constrained kinase-off state.Science signaling · 2020Article
- Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations.Communications biology · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Identification of a Kinase-Active CheA Conformation in Escherichia coli Chemoreceptor Signaling Complexes.Journal of bacteriology · 2019Article
- Conformational shifts in a chemoreceptor helical hairpin control kinase signaling inProceedings of the National Academy of Sciences of the United States of America · 2019Article
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- Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex.Journal of molecular biology · 2018Article
- Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.Scientific reports · 2017Article
- Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Journal of molecular biology · 2015Article
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- Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis.PLoS computational biology · 2015Article
- Lessons in Fundamental Mechanisms and Diverse Adaptations from the 2015 Bacterial Locomotion and Signal Transduction Meeting.Journal of bacteriology · 2015Review
- Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.Biophysical journal · 2015Article
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
- Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
The histidine kinase, CheA, couples environmental stimuli to changes in bacterial swimming behavior, converting a sensory signal to a chemical signal in the cytosol via autophosphorylation. The kinase activity is regulated in the platform of chemotaxis signaling complexes formed by CheW, chemoreceptors, and the regulatory domain of CheA. Our previous computational and mutational studies have revealed that two interdomain linkers play important roles in CheA's enzymatic activity. Of the two linkers, one that connects the dimerization and ATP binding domains is essential for both basal autophosphorylation and activation of the kinase. However, the mechanistic role of this linker remains unclear, given that it is far from the autophosphorylation reaction center (the ATP binding site). Here we investigate how this interdomain linker is coupled to CheA's enzymatic activity. Using modern nuclear magnetic resonance (NMR) techniques, we find that by interacting with the catalytic domain, the interdomain linker initiates long-range structural and dynamic changes directed toward the catalytic center of the autophosphorylation reaction. Subsequent biochemical assays define the functional relevance of these NMR-based observations. These findings extend our understanding of the chemotaxis signal transduction pathway.
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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.