ArticleJournal of the American Chemical Society2012
Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Navigating bacterial motility through chemotaxis: from molecular mechanisms to physiological perspectives.Folia microbiologica · 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
- Mechanisms of E. coli chemotaxis signaling pathways visualized using cryoET and computational approaches.Biochemical Society transactions · 2022Review
- Interdomain Linkers Regulate Histidine Kinase Activity by Controlling Subunit Interactions.Biochemistry · 2022Article
- Using Atomistic Simulations to Explore the Role of Methylation and ATP in Chemotaxis Signal Transduction.ACS omega · 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
- Article
- Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA.Journal of bacteriology · 2018Article
- Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex.Journal of molecular biology · 2018Article
- Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function.PloS one · 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
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
- Architecture and signal transduction mechanism of the bacterial chemosensory array: progress, controversies, and challenges.Current opinion in structural biology · 2014Review
- Selective allosteric coupling in core chemotaxis signaling complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Journal of the American Chemical Society · 2014Article
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5 authors.
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Abstract
A two-component signal transduction pathway underlies the phenomenon of bacterial chemotaxis that allows bacteria to modulate their swimming behavior in response to environmental stimuli. The dimeric five-domain histidine kinase, CheA, plays a central role in the pathway, converting sensory signals to a chemical signal via trans-autophosphorylation between the P1 and P4 domains. This autophosphorylation is regulated via the networked interactions among the P5 domain of CheA, CheW, and chemoreceptors. Despite a wealth of structural information about these components and their interactions, the key question of how the kinase activity of the catalytic P4 domain is regulated by the signal received from the regulatory P5 domain remains poorly understood. We performed replica exchange molecular dynamics simulations on the CheA kinase core and found that while individual domains maintained their structural fold, these domains exhibited a variety of interdomain orientations due to two interdomain linkers. A partially populated conformation that adopts an interdomain arrangement is suitable for building a functional ternary complex. An allosteric network derived from this structural model implies critical roles for two linkers in CheA's activity. The biochemical and biological functions of these linkers were assigned via a series of biochemical and genetic assays that show the P4-P5 linker controls the activation of CheA and the P3-P4 linker controls both the basal autophosphorylation activity and the activation of CheA. These results reveal the functional dependence between the two linkers and the essential role of the linkers in passing signal information from one domain to another.
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